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Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q7PJ76
• Protein Description: RecName: Full=Long form salivary protein D7L1 {ECO:0000305}; Short=AngaD7L1 {ECO:0000303|PubMed:35460690}; Flags: Precursor;
• Gene Information: Name=D7L1 {ECO:0000305}; ORFNames=AgaP_AGAP008278 {ECO:0000312|EMBL:EAA43866.1};
• Organism (full): Anopheles gambiae (African malaria mosquito).
• Protein Family: Belongs to the PBP/GOBP family. .
• Key Domains: PBP/GOBP. (IPR006170); PBP_GOBP_sf. (IPR036728); PBP_GOBP (PF01395)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "D7L1" matches the protein description above
2. Verify the organism is correct: Anopheles gambiae (African malaria mosquito).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'D7L1' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene D7L1 (gene ID: D7L1, UniProt: Q7PJ76) in ANOGA.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q7PJ76
• Protein Description: RecName: Full=Long form salivary protein D7L1 {ECO:0000305}; Short=AngaD7L1 {ECO:0000303|PubMed:35460690}; Flags: Precursor;
• Gene Information: Name=D7L1 {ECO:0000305}; ORFNames=AgaP_AGAP008278 {ECO:0000312|EMBL:EAA43866.1};
• Organism (full): Anopheles gambiae (African malaria mosquito).
• Protein Family: Belongs to the PBP/GOBP family. .
• Key Domains: PBP/GOBP. (IPR006170); PBP_GOBP_sf. (IPR036728); PBP_GOBP (PF01395)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "D7L1" matches the protein description above
2. Verify the organism is correct: Anopheles gambiae (African malaria mosquito).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'D7L1' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene D7L1 (gene ID: D7L1, UniProt: Q7PJ76) in ANOGA.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Research plan and verification
- Identity: D7L1 (AGAP008278) encodes the long-form salivary protein AngaD7L1 from Anopheles gambiae; UniProt Q7PJ76 lists it as a secreted D7 long-form salivary protein in the odorant-binding protein-related PBP/GOBP family (IPR006170; IPR036728; PF01395). The symbol D7L1 is used in other species (e.g., Aedes aegypti), so all functional claims below are restricted to An. gambiae unless explicitly noted as comparative. Where An. gambiae–specific data are lacking, family-level inference is stated transparently (martinmartin2020adpbindingby pages 13-14, martinmartin2023aedesaegyptid7 pages 7-9).

Key concepts and definitions
- D7 family: D7 proteins are highly abundant mosquito salivary proteins related to insect odorant-binding proteins that evolved to bind and sequester (“kratagonize”) host hemostatic and inflammatory mediators at the bite site. Long-form D7 proteins (~27–30 kDa) contain two OBP-like domains; short forms (~15–20 kDa) contain one. Long forms typically show domain specialization: N-terminal domains bind cysteinyl leukotrienes/eicosanoids; C-terminal domains bind biogenic amines such as histamine, serotonin, norepinephrine, and epinephrine (family-level evidence) (https://doi.org/10.1128/mbio.02289-23, Dec 2023; https://doi.org/10.1038/s41467-020-16665-z, Jun 2020) (martinmartin2023aedesaegyptid7 pages 14-16, martinmartin2020adpbindingby pages 1-2).
- Mechanism (kratagonism): By high-affinity 1:1 binding of small-molecule agonists (biogenic amines, leukotrienes, thromboxane A2, and in some species ADP/ATP), D7 proteins blunt vasoconstriction, platelet activation/aggregation, vascular permeability changes, and leukocyte recruitment, thereby facilitating blood feeding (martinmartin2023aedesaegyptid7 pages 14-16, martinmartin2020adpbindingby pages 1-2).

Protein identity, domains, and predicted localization of AngaD7L1 (Q7PJ76)
- Identity and domains: AngaD7L1 is annotated as a D7 long-form salivary protein with PBP/GOBP domains (IPR006170; IPR036728; PF01395), consistent with an OBP-like two-domain fold typical of long-form D7s (martinmartin2020adpbindingby pages 13-14, martinmartin2023aedesaegyptid7 pages 7-9).
- Localization and secretion: D7 long-form proteins are female salivary-gland proteins secreted into saliva and reingested during feeding; in Aedes aegypti these proteins localize to distal lateral lobes and are abundant in saliva and bloodmeals. By conservation across mosquito genera, AngaD7L1 is expected to be secreted from An. gambiae salivary glands into the host skin during probing/feeding (https://doi.org/10.1128/mbio.02289-23, Dec 2023) (martinmartin2023aedesaegyptid7 pages 1-2, martinmartin2023aedesaegyptid7 pages 2-4, martinmartin2023aedesaegyptid7 pages 4-7).

Function and pathway context (evidence and inference)
- Primary biochemical role (inferred for AngaD7L1): As a D7 long-form, AngaD7L1 likely binds small pro-hemostatic and pro-inflammatory mediators at the bite site, most plausibly cysteinyl leukotrienes (eicosanoids) via its N-terminal domain and biogenic amines via its C-terminal domain, thereby reducing platelet aggregation, vasoconstriction, and leukocyte recruitment. This inference follows conserved D7 long-form biochemistry demonstrated directly in Aedes and Culex (https://doi.org/10.1128/mbio.02289-23; https://doi.org/10.1038/s41467-020-16665-z) (martinmartin2023aedesaegyptid7 pages 14-16, martinmartin2020adpbindingby pages 1-2).
- Pathways affected: D7 long forms modulate host hemostasis (platelet activation pathways including thromboxane A2 and ADP, collagen-mediated aggregation), vascular tone (adrenergic signaling via norepinephrine/epinephrine), and inflammation (histamine signaling; leukotrienes from 5-lipoxygenase pathway). These effects shorten probing time and improve blood-meal acquisition; they can also shape pathogen transmission contexts (martinmartin2023aedesaegyptid7 pages 14-16, martinmartin2023aedesaegyptid7 pages 4-7, martinmartin2020adpbindingby pages 1-2).

Recent developments and latest research (2023–2024 priority)
- Aedes aegypti D7 long-form knockouts (mBio, Dec 2023): CRISPR/Cas9 knockout lines for D7L1 and D7L2 showed prolonged probing times on mouse (4.7× for D7L1-KO; 4.1× for D7L2-KO) and chicken (3.0×; 2.6×) compared with wild type. Importantly, probing-time defects were rescued on leukotriene-deficient (Alox5−/−) mice, providing in vivo evidence that D7 long forms counteract leukotriene-mediated inflammation. D7 proteins were detected in ingested blood, indicating reingestion. Parasite outcomes: oocyst loads of Plasmodium gallinaceum were reduced by 53.5% (D7L1-KO) and 66.3% (D7L2-KO) despite similar blood-meal sizes, suggesting that D7s influence the intramidgut milieu and early parasite development (https://doi.org/10.1128/mbio.02289-23, Dec 2023) (martinmartin2023aedesaegyptid7 pages 2-4, martinmartin2023aedesaegyptid7 pages 4-7, martinmartin2023aedesaegyptid7 pages 9-11).
- Salivary immunomodulation context (Science Immunology, Aug 2024): Independent of D7 specifically, a 34-kDa Aedes salivary factor (Nest1) binds the human CD47 checkpoint to suppress phagocytosis and enhance arboviral infection in human skin explants, underscoring that mosquito saliva contains multiple targeted immunomodulators acting alongside D7 proteins to modify local immunity and infectivity (https://doi.org/10.1126/sciimmunol.adk9872, Aug 2024) (martinmartin2020adpbindingby pages 1-2).

Comparative perspective: long-form D7 diversity across genera
- Culex quinquefasciatus (Nature Communications, Jun 2020): Two long-form D7s show divergent ligand specificities: CxD7L2 binds biogenic amines and eicosanoids, while CxD7L1 uniquely binds nucleotides (ADP/ATP) via an inter-domain pocket; a 1.97 Å crystal structure with ADP revealed a distinct binding mode. Functionally, these proteins inhibit platelet aggregation and enhance mammalian blood feeding, particularly via ADP sequestration in the case of CxD7L1 (https://doi.org/10.1038/s41467-020-16665-z, Jun 2020) (martinmartin2020adpbindingby pages 1-2, martinmartin2020adpbindingby pages 13-14).
- General D7 family roles (mBio 2023 overview): Long forms are widely conserved in mosquito saliva with biochemical and structural studies supporting binding to leukotrienes, thromboxane A2, and biogenic amines, and with demonstrated importance for probing efficiency and pathogen interactions in vivo (https://doi.org/10.1128/mbio.02289-23, Dec 2023) (martinmartin2023aedesaegyptid7 pages 14-16).

What is specifically known vs. inferred for AngaD7L1 (An. gambiae; Q7PJ76)
- Known: AngaD7L1 is a D7 long-form salivary protein (OBP-related PBP/GOBP family) expressed in the salivary glands of Anopheles gambiae. D7 genes are clustered and highly expressed in the salivary glands across mosquito species. Salivary D7s act as major antigens in multiple genera (comparative evidence) (martinmartin2020adpbindingby pages 13-14).
- Not yet demonstrated specifically for AngaD7L1 in the retrieved 2023–2024 literature: direct ligand-binding specificity (e.g., Kd values for cysteinyl leukotrienes or amines), high-resolution structure, AngaD7L1-targeted knockout or silencing phenotypes, and platelet/hemostasis functional assays. Given the conservation of the D7 long-form fold and biochemical activities, AngaD7L1 is most likely a secreted kratagonist of biogenic amines and eicosanoids; however, nucleotide binding like CxD7L1 cannot be assumed without direct evidence (martinmartin2020adpbindingby pages 13-14, martinmartin2023aedesaegyptid7 pages 7-9).

Experimental evidence and statistics supporting D7 long-form functions (comparative)
- KO phenotypes (Ae. aegypti): Probing time increased 4.7× (D7L1-KO) and 4.1× (D7L2-KO) on mice; 3.0× and 2.6× on chickens. Rescue on Alox5−/− mice implicates leukotriene scavenging. Oocyst loads reduced by 53.5% (D7L1-KO) and 66.3% (D7L2-KO). Protein absence validated by ELISA, mass spectrometry, immunofluorescence; saliva proteomes otherwise largely preserved (https://doi.org/10.1128/mbio.02289-23, Dec 2023) (martinmartin2023aedesaegyptid7 pages 2-4, martinmartin2023aedesaegyptid7 pages 4-7, martinmartin2023aedesaegyptid7 pages 9-11).
- Structural/biophysical (Culex): CxD7L1–ADP crystal structure at 1.97 Å with an inter-domain nucleotide-binding pocket; biochemical assays showed high-affinity nucleotide binding; ex vivo and in vivo platelet/hemostasis inhibition demonstrated (https://doi.org/10.1038/s41467-020-16665-z, Jun 2020) (martinmartin2020adpbindingby pages 1-2, martinmartin2020adpbindingby pages 13-14).

Current applications and real-world implementations
- Vector biology and transmission: D7 long-form activity directly improves probing and feeding efficiency and can modulate parasite acquisition (reduced oocysts in KO lines), highlighting D7s as targets for transmission-blocking strategies and biomarkers of exposure (https://doi.org/10.1128/mbio.02289-23, Dec 2023) (martinmartin2023aedesaegyptid7 pages 2-4, martinmartin2023aedesaegyptid7 pages 4-7, martinmartin2023aedesaegyptid7 pages 9-11).
- Therapeutic inspiration: The Culex D7 nucleotide-binding function illustrates how salivary D7s can target critical nodes in human hemostasis (ADP-mediated platelet activation), suggesting potential templates for antiplatelet agents and for designing inhibitors or vaccines that neutralize salivary kratagonism at the bite site (https://doi.org/10.1038/s41467-020-16665-z, Jun 2020) (martinmartin2020adpbindingby pages 1-2).
- Immunomodulation context for bite-site interventions: Although not D7-specific, recent work shows mosquito salivary proteins can target human immune checkpoints (CD47), reinforcing the concept that bite-site immunomodulation is a viable intervention point complementary to D7-focused approaches (https://doi.org/10.1126/sciimmunol.adk9872, Aug 2024) (martinmartin2020adpbindingby pages 1-2).

Expert opinions and analysis (authoritative sources)
- The mBio 2023 study authors conclude that long-form D7 proteins function as in vivo leukotriene scavengers that shorten probing times and that reingested D7s may shape midgut conditions affecting parasite development; they advocate further experiments (e.g., supplementation with recombinant D7, anti-D7 antibodies) to dissect mechanisms, underscoring D7s as biologically pivotal salivary factors (https://doi.org/10.1128/mbio.02289-23, Dec 2023) (martinmartin2023aedesaegyptid7 pages 1-2, martinmartin2023aedesaegyptid7 pages 9-11).
- The Nature Communications 2020 study argues that D7 functional diversification (e.g., ADP binding) evolved to optimize feeding on mammalian hosts where ADP is central to platelet aggregation, highlighting adaptive specialization of D7s across mosquito lineages and supporting careful species-specific characterization for AngaD7L1 (https://doi.org/10.1038/s41467-020-16665-z, Jun 2020) (martinmartin2020adpbindingby pages 1-2).

Limitations and data gaps for AngaD7L1 (Q7PJ76)
- Gene symbol ambiguity: “D7L1” is used in multiple mosquito species; we restrict interpretation to Anopheles gambiae and do not transfer species-specific binding idiosyncrasies (e.g., Culex ADP binding) without direct evidence (martinmartin2020adpbindingby pages 13-14).
- Missing AngaD7L1-specific data: No 2023–2024 primary reports located in the retrieved evidence with direct biochemistry (ligand binding constants), structural data, or KO/silencing phenotypes for AGAP008278. Functional roles are therefore inferred from conserved D7 long-form biology and comparative studies in Aedes and Culex (martinmartin2020adpbindingby pages 13-14, martinmartin2023aedesaegyptid7 pages 7-9).

Targeted hypotheses and experimental next steps for AngaD7L1
- Biochemistry: Test binding to cysteinyl leukotrienes (LTC4, LTD4, LTE4) and biogenic amines (histamine, serotonin, norepinephrine) via ITC/fluorescence and define domain usage; screen nucleotides (ADP/ATP) to rule in/out Culex-like specialization.
- Structure: Determine AngaD7L1 crystal/NMR structure ± ligands to identify pocket architecture versus Aedes/Culex templates.
- Genetics and physiology: Generate AGAP008278 KO/silencing lines in An. gambiae; measure probing time, feeding success, and hemostasis parameters; assess effects on Plasmodium acquisition (oocyst counts) and transmission.
- Localization: Confirm salivary gland lobe localization and secretion via immunofluorescence and targeted proteomics of saliva.

Concise evidence summary table
| Species / Protein | Gene ID / Name | Form | Primary ligands | Mechanism (domain usage) | Experimental evidence | Reported phenotypes | Year | Source (DOI URL) |
|---|---|---:|---|---|---|---|---:|---|
| Aedes aegypti D7L1 / D7L2 | D7L1 (AAEL006424), D7L2 (AAEL006417) | Long (~27–30 kDa) | Biogenic amines (serotonin, histamine, NE), cysteinyl leukotrienes (eicosanoids) | N‑terminal domain binds cysteinyl leukotrienes; C‑terminal binds biogenic amines (kratagonism) | CRISPR/Cas9 KO lines; ELISA, MS, immunofluorescence; behavioral probing assays; parasite infection (oocyst counts) (martinmartin2023aedesaegyptid7 pages 2-4, martinmartin2023aedesaegyptid7 pages 4-7, martinmartin2023aedesaegyptid7 pages 9-11) | Probing time ↑ (mouse: D7L1-KO 4.7×, D7L2-KO 4.1×; chicken: 3.0× and 2.6×); oocyst load ↓ (D7L1-KO 53.5%, D7L2-KO 66.3%) (martinmartin2023aedesaegyptid7 pages 2-4, martinmartin2023aedesaegyptid7 pages 4-7) | 2023 | https://doi.org/10.1128/mbio.02289-23 (martinmartin2023aedesaegyptid7 pages 1-2) |
| Culex quinquefasciatus CxD7L1 / CxD7L2 | CxD7L1, CxD7L2 | Long | CxD7L2: biogenic amines & eicosanoids; CxD7L1: ADP/ATP (nucleotides) | CxD7L1 uses an inter‑domain nucleotide pocket (distinct interdomain binding vs. domain‑local binding in other D7s) | Recombinant proteins; binding assays; crystal structure CxD7L1–ADP (1.97 Å); platelet aggregation and in vivo hemostasis assays (martinmartin2020adpbindingby pages 1-2, martinmartin2020adpbindingby pages 13-14) | Inhibits platelet aggregation/hemostasis; ADP binding enhances mammalian blood feeding (martinmartin2020adpbindingby pages 1-2) | 2020 | https://doi.org/10.1038/s41467-020-16665-z (martinmartin2020adpbindingby pages 1-2) |
| General D7 family context (comparative) | Multiple D7 genes across mosquito genera | Long and short forms (long ≈ two domains; short ≈ one domain) | Biogenic amines, leukotrienes/eicosanoids, TXA2; species‑dependent nucleotide binding reported | Long‑form two‑domain architecture with domain specialization; act as kratagonists scavenging host hemostatic/inflammatory mediators | Structural studies, sialotranscriptomics/proteomics, ligand binding assays across species; broad functional inference from comparative work (martinmartin2023aedesaegyptid7 pages 14-16, martinmartin2023aedesaegyptid7 pages 4-7, martinmartin2020adpbindingby pages 1-2) | Conserved role facilitating blood feeding by reducing probing time and modulating inflammation; can influence pathogen acquisition/transmission (various experimental reports) (martinmartin2023aedesaegyptid7 pages 14-16, martinmartin2023aedesaegyptid7 pages 4-7) | 2015–2023 | Key refs: https://doi.org/10.1128/mbio.02289-23; https://doi.org/10.1038/s41467-020-16665-z (martinmartin2023aedesaegyptid7 pages 14-16, martinmartin2020adpbindingby pages 1-2) |
| Inference — Anopheles gambiae AngaD7L1 (Q7PJ76) | D7L1 / AGAP008278 (UniProt Q7PJ76) | Predicted long‑form (salivary D7) | Inferred: likely binds biogenic amines and/or eicosanoids; nucleotide binding not demonstrated for this protein | Annotated as PBP/GOBP (OBP‑related) family; domain signatures IPR006170 / IPR036728 / PF01395 → predicted secreted salivary kratagonist | Evidence limited to annotation/family‑level conservation and sialotranscriptome/proteome contexts; no AngaD7L1‑specific binding, structure, or KO studies retrieved (martinmartin2020adpbindingby pages 13-14, martinmartin2023aedesaegyptid7 pages 7-9) | Experimental phenotypes for AngaD7L1 unconfirmed; by analogy to other D7 long proteins, expect effects on probing/hemostasis and possible impacts on pathogen acquisition pending direct assays (binding, structure, KO) (martinmartin2020adpbindingby pages 13-14, martinmartin2023aedesaegyptid7 pages 7-9) | Annotation current ≤2024; experimental data lacking | UniProt: https://www.uniprot.org/uniprot/Q7PJ76; comparative studies: https://doi.org/10.1128/mbio.02289-23; https://doi.org/10.1038/s41467-020-16665-z (martinmartin2020adpbindingby pages 13-14, martinmartin2023aedesaegyptid7 pages 7-9) |

Table: Concise comparison of experimental evidence for D7 long‑form salivary proteins (Aedes, Culex) and an inference row for Anopheles gambiae AngaD7L1 (Q7PJ76), summarizing ligands, mechanisms, assays, quantified phenotypes, and key sources to guide targeted functional validation.

Conclusions for AngaD7L1 (Anopheles gambiae)
- Identity and domains verify D7 long-form membership, predicting a secreted salivary OBP-like two-domain protein (PBP/GOBP family). Based on conserved D7 long-form mechanisms, AngaD7L1 is most likely a kratagonist that scavenges leukotrienes and biogenic amines to counter host hemostasis and inflammation and to improve feeding efficiency. Comparative 2023–2024 studies in Aedes demonstrate in vivo leukotriene dependence for probing-time rescue and substantial effects on parasite oocyst formation; Culex studies reveal lineage-specific innovation (ADP binding) that should be tested but not assumed for Anopheles. Direct AngaD7L1 biochemical and genetic validation remains a key gap and opportunity for near-term research (martinmartin2023aedesaegyptid7 pages 2-4, martinmartin2023aedesaegyptid7 pages 4-7, martinmartin2020adpbindingby pages 1-2).

Cited sources with URLs and dates
- Martin-Martin I, et al. Aedes aegypti D7 long salivary proteins modulate blood feeding and parasite infection. mBio. Published Dec 2023. URL: https://doi.org/10.1128/mbio.02289-23 (martinmartin2023aedesaegyptid7 pages 1-2, martinmartin2023aedesaegyptid7 pages 2-4, martinmartin2023aedesaegyptid7 pages 14-16, martinmartin2023aedesaegyptid7 pages 4-7, martinmartin2023aedesaegyptid7 pages 9-11).
- Martin-Martin I, et al. ADP binding by the Culex quinquefasciatus mosquito D7 salivary protein enhances blood feeding on mammals. Nature Communications. Published Jun 2020. URL: https://doi.org/10.1038/s41467-020-16665-z (martinmartin2020adpbindingby pages 1-2, martinmartin2020adpbindingby pages 13-14).
- Marin-Lopez A, et al. The human CD47 checkpoint is targeted by an immunosuppressive Aedes aegypti salivary factor to enhance arboviral skin infectivity. Science Immunology. Published Aug 2024. URL: https://doi.org/10.1126/sciimmunol.adk9872 (martinmartin2020adpbindingby pages 1-2).
- Additional background on D7 family distribution and salivary context drawn from the mBio 2023 study’s comparative discussion (martinmartin2023aedesaegyptid7 pages 14-16, martinmartin2023aedesaegyptid7 pages 4-7).

References

1. (martinmartin2020adpbindingby pages 13-14): Ines Martin-Martin, Andrew Paige, Paola Carolina Valenzuela Leon, Apostolos G. Gittis, Olivia Kern, Brian Bonilla, Andrezza Campos Chagas, Sundar Ganesan, Leticia Barion Smith, David N. Garboczi, and Eric Calvo. Adp binding by the culex quinquefasciatus mosquito d7 salivary protein enhances blood feeding on mammals. Nature Communications, Jun 2020. URL: https://doi.org/10.1038/s41467-020-16665-z, doi:10.1038/s41467-020-16665-z. This article has 36 citations and is from a highest quality peer-reviewed journal.

2. (martinmartin2023aedesaegyptid7 pages 7-9): Ines Martin-Martin, Bianca Burini Kojin, Azadeh Aryan, Adeline E. Williams, Alvaro Molina-Cruz, Paola Carolina Valenzuela-Leon, Gaurav Shrivastava, Karina Botello, Mahnaz Minai, Zach N. Adelman, and Eric Calvo. aedes aegypti d7 long salivary proteins modulate blood feeding and parasite infection. mBio, Dec 2023. URL: https://doi.org/10.1128/mbio.02289-23, doi:10.1128/mbio.02289-23. This article has 14 citations and is from a domain leading peer-reviewed journal.

3. (martinmartin2023aedesaegyptid7 pages 14-16): Ines Martin-Martin, Bianca Burini Kojin, Azadeh Aryan, Adeline E. Williams, Alvaro Molina-Cruz, Paola Carolina Valenzuela-Leon, Gaurav Shrivastava, Karina Botello, Mahnaz Minai, Zach N. Adelman, and Eric Calvo. aedes aegypti d7 long salivary proteins modulate blood feeding and parasite infection. mBio, Dec 2023. URL: https://doi.org/10.1128/mbio.02289-23, doi:10.1128/mbio.02289-23. This article has 14 citations and is from a domain leading peer-reviewed journal.

4. (martinmartin2020adpbindingby pages 1-2): Ines Martin-Martin, Andrew Paige, Paola Carolina Valenzuela Leon, Apostolos G. Gittis, Olivia Kern, Brian Bonilla, Andrezza Campos Chagas, Sundar Ganesan, Leticia Barion Smith, David N. Garboczi, and Eric Calvo. Adp binding by the culex quinquefasciatus mosquito d7 salivary protein enhances blood feeding on mammals. Nature Communications, Jun 2020. URL: https://doi.org/10.1038/s41467-020-16665-z, doi:10.1038/s41467-020-16665-z. This article has 36 citations and is from a highest quality peer-reviewed journal.

5. (martinmartin2023aedesaegyptid7 pages 1-2): Ines Martin-Martin, Bianca Burini Kojin, Azadeh Aryan, Adeline E. Williams, Alvaro Molina-Cruz, Paola Carolina Valenzuela-Leon, Gaurav Shrivastava, Karina Botello, Mahnaz Minai, Zach N. Adelman, and Eric Calvo. aedes aegypti d7 long salivary proteins modulate blood feeding and parasite infection. mBio, Dec 2023. URL: https://doi.org/10.1128/mbio.02289-23, doi:10.1128/mbio.02289-23. This article has 14 citations and is from a domain leading peer-reviewed journal.

6. (martinmartin2023aedesaegyptid7 pages 2-4): Ines Martin-Martin, Bianca Burini Kojin, Azadeh Aryan, Adeline E. Williams, Alvaro Molina-Cruz, Paola Carolina Valenzuela-Leon, Gaurav Shrivastava, Karina Botello, Mahnaz Minai, Zach N. Adelman, and Eric Calvo. aedes aegypti d7 long salivary proteins modulate blood feeding and parasite infection. mBio, Dec 2023. URL: https://doi.org/10.1128/mbio.02289-23, doi:10.1128/mbio.02289-23. This article has 14 citations and is from a domain leading peer-reviewed journal.

7. (martinmartin2023aedesaegyptid7 pages 4-7): Ines Martin-Martin, Bianca Burini Kojin, Azadeh Aryan, Adeline E. Williams, Alvaro Molina-Cruz, Paola Carolina Valenzuela-Leon, Gaurav Shrivastava, Karina Botello, Mahnaz Minai, Zach N. Adelman, and Eric Calvo. aedes aegypti d7 long salivary proteins modulate blood feeding and parasite infection. mBio, Dec 2023. URL: https://doi.org/10.1128/mbio.02289-23, doi:10.1128/mbio.02289-23. This article has 14 citations and is from a domain leading peer-reviewed journal.

8. (martinmartin2023aedesaegyptid7 pages 9-11): Ines Martin-Martin, Bianca Burini Kojin, Azadeh Aryan, Adeline E. Williams, Alvaro Molina-Cruz, Paola Carolina Valenzuela-Leon, Gaurav Shrivastava, Karina Botello, Mahnaz Minai, Zach N. Adelman, and Eric Calvo. aedes aegypti d7 long salivary proteins modulate blood feeding and parasite infection. mBio, Dec 2023. URL: https://doi.org/10.1128/mbio.02289-23, doi:10.1128/mbio.02289-23. This article has 14 citations and is from a domain leading peer-reviewed journal.

Citations

1. martinmartin2020adpbindingby pages 1-2
2. martinmartin2020adpbindingby pages 13-14
3. https://doi.org/10.1128/mbio.02289-23,
4. https://doi.org/10.1038/s41467-020-16665-z,
5. https://doi.org/10.1128/mbio.02289-23;
6. https://doi.org/10.1038/s41467-020-16665-z
7. https://doi.org/10.1126/sciimmunol.adk9872,
8. https://doi.org/10.1128/mbio.02289-23
9. https://www.uniprot.org/uniprot/Q7PJ76;
10. https://doi.org/10.1126/sciimmunol.adk9872