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gene_id: PGRPS3
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gene_info: Name=PGRPS3 {ECO:0000313|EMBL:ADA54937.1};
organism_full: Anopheles gambiae (African malaria mosquito).
protein_family: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
protein_domains: Amidase/PGRP_sf. (IPR036505); Amidase_domain. (IPR002502); Peptidoglycan_recognition.
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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: D2STP8
• Protein Description: RecName: Full=Peptidoglycan-recognition protein {ECO:0000256|PIRNR:PIRNR037945};
• Gene Information: Name=PGRPS3 {ECO:0000313|EMBL:ADA54937.1};
• Organism (full): Anopheles gambiae (African malaria mosquito).
• Protein Family: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
• Key Domains: Amidase/PGRP_sf. (IPR036505); Amidase_domain. (IPR002502); Peptidoglycan_recognition. (IPR017331); PGRP. (IPR015510); PGRP_domain_met/bac. (IPR006619)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "PGRPS3" 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 'PGRPS3' 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 PGRPS3 (gene ID: PGRPS3, UniProt: D2STP8) 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: D2STP8
• Protein Description: RecName: Full=Peptidoglycan-recognition protein {ECO:0000256|PIRNR:PIRNR037945};
• Gene Information: Name=PGRPS3 {ECO:0000313|EMBL:ADA54937.1};
• Organism (full): Anopheles gambiae (African malaria mosquito).
• Protein Family: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
• Key Domains: Amidase/PGRP_sf. (IPR036505); Amidase_domain. (IPR002502); Peptidoglycan_recognition. (IPR017331); PGRP. (IPR015510); PGRP_domain_met/bac. (IPR006619)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "PGRPS3" 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 'PGRPS3' 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 PGRPS3 (gene ID: PGRPS3, UniProt: D2STP8) 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.

Comprehensive research report: Anopheles gambiae PGRP-S3 (UniProt D2STP8)

Executive verification and scope statement
- Identity and organism: PGRPS3 in Anopheles gambiae corresponds to a short peptidoglycan-recognition protein (PGRP), annotated in UniProt as an amidase-family member. The symbol matches the PGRP short-class nomenclature used for Anopheles (PGRP-S1, -S2, -S3) and is not to be confused with similarly named genes in other taxa (honeybee, silkworm). Literature directly specific to A. gambiae PGRP-S3 is limited; several studies consider the short paralogs S2 and S3 together due to high sequence similarity. Inferences below rely on Anopheles-focused reviews and analyses that discuss the short PGRPs collectively, together with evolutionary and pathway evidence pointing to amidase-type function for S2/S3 (see citations). Where the evidence is indirect, this is stated explicitly (meister2009anophelesgambiaepgrplcmediated pages 7-9, mendes2010molecularevolutionof pages 3-7, zakovic2017nfκblikesignalingpathway pages 2-4, audi2025apgrplc1rel2faxis pages 18-20).

1) Key concepts and definitions with current understanding
- PGRPs in insects: Peptidoglycan-recognition proteins are pattern-recognition proteins that bind bacterial peptidoglycan (PGN) and either signal to activate immune pathways or enzymatically cleave PGN to modulate signaling. Short PGRPs (PGRP-S) are typically extracellular/secreted proteins, whereas long PGRPs (PGRP-L) include membrane/cytosolic signaling receptors (e.g., PGRP-LC) (zakovic2017nfκblikesignalingpathway pages 2-4, moussawi2019functionalandmolecular pages 24-28).
- Pathway context in Anopheles: The IMD/REL2 pathway is the principal NF-κB-like antibacterial signaling cascade in A. gambiae; it is triggered by PGN sensing via PGRP-LC and regulates antimicrobial peptide responses and microbiota homeostasis. Toll signaling also contributes, but PGRP-LC is the core receptor for PGN sensing with broad binding to both Lys- and DAP-type PGN in mosquitoes, in contrast to Drosophila (zakovic2017nfκblikesignalingpathway pages 2-4, meister2009anophelesgambiaepgrplcmediated pages 7-9).
- Short PGRPs S2/S3: Evolutionary analysis of A. gambiae and A. arabiensis shows PGRP-S2 and PGRP-S3 are autosomal paralogs under purifying selection, with high haplotype diversity for PGRP-S3 but Ka/Ks < 1, consistent with conserved biochemical constraints. PGRP-S1 differs in genomic location (X chromosome) and selection signatures (mendes2010molecularevolutionof pages 3-7).

2) Protein domain architecture, catalytic features, and predicted biochemical function
- Domain/family: PGRP-S3 belongs to the N-acetylmuramoyl-L-alanine amidase 2 family and harbors a PGRP amidase domain. This family includes Zn2+-dependent amidases that hydrolyze the lactyl-amide bond between MurNAc and L-Ala in PGN, thereby degrading muropeptides and dampening IMD signaling when secreted (insect exemplars: PGRP-LB/-SC in Drosophila). In Anopheles, short PGRPs are characterized as small extracellular PGRPs, consistent with negative regulatory amidases (inference supported by reviews) (zakovic2017nfκblikesignalingpathway pages 2-4, moussawi2019functionalandmolecular pages 24-28).
- Catalytic residues/metal binding: Direct residue-level mapping for A. gambiae PGRP-S3 has not been experimentally resolved in the cited sources; however, recent analyses discussing Anopheles PGRPs indicate that short PGRPs S2 and S3 retain the canonical amidase signature motif(s) characteristic of Zn2+-dependent N-acetylmuramoyl-L-alanine amidases, supporting predicted catalytic activity (prediction; see recent pathway-focused work) (audi2025apgrplc1rel2faxis pages 18-20).
- Substrate specificity: The IMD pathway in mosquitoes can be triggered by both DAP- and Lys-type PGN via PGRP-LC, and amidase-type PGRPs often display selectivity toward specific PGN types in other insects. For PGRP-S3, direct biochemical specificity data were not found in the retrieved Anopheles-focused literature; we therefore infer potential activity toward muropeptides (DAP and/or Lys type) by homology to amidase-type PGRPs. This is a reasoned inference pending direct assay data (zakovic2017nfκblikesignalingpathway pages 2-4, audi2025apgrplc1rel2faxis pages 18-20).

3) Cellular localization, expression, and pathway role
- Localization: Short PGRPs are described as small extracellular (secreted) PGRPs in insects, distinguishing them from transmembrane/cytosolic long PGRPs. PGRP-S3, as a short PGRP, is therefore most likely secreted into the hemolymph or local extracellular spaces where it can bind and/or hydrolyze PGN (inference based on class properties) (moussawi2019functionalandmolecular pages 24-28, zakovic2017nfκblikesignalingpathway pages 2-4).
- Expression and regulation: Genome/transcriptome studies and functional work in Anopheles show robust immune regulation of PGRP family members during bacterial challenges and after blood feeding, which expands gut microbiota and stimulates IMD signaling. Specific tissue-expression datasets for PGRP-S3 were not identified in the provided context; nevertheless, S-class PGRPs are generally part of the humoral response and expected to be upregulated upon bacterial challenge (inference grounded in mosquito immunity reviews) (zakovic2017nfκblikesignalingpathway pages 2-4, meister2009anophelesgambiaepgrplcmediated pages 7-9, moussawi2019functionalandmolecular pages 24-28).
- Pathway role: In A. gambiae, PGRP-LC is the principal IMD receptor sensing PGN and controlling microbiota and antibacterial defenses; short amidase-type PGRPs act as modulators by scavenging PGN, thereby shaping the amplitude/duration of IMD activation. Given the conserved signatures and evolutionary constraints on S2/S3, PGRP-S3 likely functions as an extracellular PGN amidase (negative regulator) rather than a transmembrane signaling receptor (inference) (zakovic2017nfκblikesignalingpathway pages 2-4, mendes2010molecularevolutionof pages 3-7, audi2025apgrplc1rel2faxis pages 18-20).

4) Genetic evidence and phenotypes (bacterial challenge, Plasmodium infection)
- Paralogs S2/S3 co-silencing: Functional mosquito work commonly targeted PGRP-S2 and PGRP-S3 together because of near-identical sequences, complicating assignment of phenotypes to S3 alone. In the context of PGRP-LC-mediated responses, the canonical signaling receptor (LC) governs survival to both Gram-negative and Gram-positive systemic infection and modulates Plasmodium infection intensities; the short PGRPs (including S2/S3) are discussed as modulators rather than primary receptors (meister2009anophelesgambiaepgrplcmediated pages 7-9).
- Evolutionary constraints and function: Population genetic analyses demonstrate that PGRP-S2/S3 are under purifying selection with Ka/Ks < 1 and extensive haplotype diversity for PGRP-S3 (43 haplotypes in the surveyed East African populations), indicating functional constraint and longstanding roles in antibacterial recognition/modulation rather than rapidly diversifying immune receptors. AMOVA/Fst analyses show little species-level structure for S2/S3, consistent with conserved function across Anopheles taxa (mendes2010molecularevolutionof pages 3-7).
- Link to Plasmodium interactions (indirect): PGRP-LC signaling impacts midgut microbiota after blood feeding and thereby modulates Plasmodium infection levels, with microbiota clearance increasing parasite loads and bacterial feeding enhancing resistance in a PGRP-LC-dependent manner. While this places PGRP-LC at the center of bacteria–parasite crosstalk, S-class PGRPs such as S3 likely contribute by tuning the availability of muropeptide ligands that engage IMD signaling. Direct RNAi phenotypes for PGRP-S3 alone were not reported in the provided sources (meister2009anophelesgambiaepgrplcmediated pages 7-9, zakovic2017nfκblikesignalingpathway pages 2-4).

5) Recent developments and latest research (priority 2023–2024)
- The Anopheles IMD/REL2 pathway continues to be refined as a key regulator of midgut bacterial homeostasis and anti-pathogen defense. Recent work discussing Anopheles PGRP modules and REL2 emphasizes that short PGRPs S2/S3 retain amidase signatures, supporting their role as enzymatic modulators rather than primary receptors. However, explicit 2023–2024 experimental dissection of PGRP-S3 alone in A. gambiae was not recovered in the present evidence set; we therefore highlight this as an open area where targeted CRISPR/RNAi or recombinant biochemical assays would be valuable (audi2025apgrplc1rel2faxis pages 18-20).

6) Current applications and real-world implementations
- Vector control relevance: Modulating IMD/REL2 signaling alters both survival to systemic bacterial infection and Plasmodium infection intensities. Because PGRP-S3 likely shapes PGN availability and IMD tone as an extracellular amidase, S3 is a plausible lever for tuning basal immune responsiveness and microbiota homeostasis, with potential downstream effects on malaria transmission. Practically, current implementations focus on manipulating PGRP-LC/REL2 pathway activity; translating S3 modulation into interventions would require validating its enzymatic role and targetability (meister2009anophelesgambiaepgrplcmediated pages 7-9, zakovic2017nfκblikesignalingpathway pages 2-4).

7) Expert opinions and analysis from authoritative sources
- Reviews and comparative analyses concur that Anopheles IMD/REL2 immunity integrates broad PGN sensing via PGRP-LC and modulation by extracellular PGRPs. In this framework, short PGRPs S2/S3 are best viewed as conserved, secreted amidases that fine-tune signaling, analogous to Drosophila PGRP-LB/SC. The evolutionary purifying selection on S3 supports a conserved biochemical role rather than rapidly evolving specificity determinants (zakovic2017nfκblikesignalingpathway pages 2-4, mendes2010molecularevolutionof pages 3-7).

8) Relevant statistics and data from recent studies
- Haplotype diversity and selection: PGRP-S3 presented 43 haplotypes across sampled A. gambiae and A. arabiensis populations from East Africa, with Ka/Ks < 1 and AMOVA showing limited interspecific structure (e.g., Fct ≈ 0.089; Fst ≈ 0.192), consistent with purifying selection and functional conservation. PGRP-S2 showed similar constraints, whereas PGRP-S1 showed stronger divergence linked to X-chromosome location (details in Mendes et al. 2010) (mendes2010molecularevolutionof pages 3-7).
- Pathway breadth: Structural and functional analyses indicate Anopheles PGRP-LC binds both Lys- and DAP-type PGN and is critical for survival to Gram-negative and Gram-positive bacteria; this broadness contrasts Drosophila PGRP-LC’s DAP preference and frames how short PGRPs like S3 would modulate signaling in mosquitoes (zakovic2017nfκblikesignalingpathway pages 2-4, meister2009anophelesgambiaepgrplcmediated pages 7-9).

Embedded source summary table
| Citation ID | Reference (first author, year, title) | Outlet | URL / DOI | Organism focus | Key relevance to PGRP-S3 / function |
|---|---|---|---|---|---|
| pqac-00000000 | Moussawi LH El, 2019, Functional and molecular characterization of the serine protease homologue CLIPA28 in the melanization response of Anopheles gambiae | Unknown journal | (no DOI/URL in context) | Anopheles gambiae | Provides general mosquito immune context and summarizes PGRP family roles (short vs long PGRPs; amidase-type PGRPs as extracellular regulators), useful background though not S3-specific. |
| pqac-00000001 | Audi A, 2025, A PGRPLC1/Rel2-F axis controls Anopheles gambiae resistance to systemic infections with Gram-positive bacteria containing Lys-type peptidoglycan | PLOS Pathogens | https://doi.org/10.1371/journal.ppat.1013527 | Anopheles gambiae | Recent analysis of PGRP/Rel2 signaling modules; notes predictions about short PGRPs (PGRP-S2/S3) amidase signatures and places PGRPs in Imd/Rel2 context. |
| pqac-00000002 | Zakovic S & Levashina EA, 2017, NF-κB-Like Signaling Pathway REL2 in Immune Defenses of the Malaria Vector Anopheles gambiae | Frontiers in Cellular and Infection Microbiology | https://doi.org/10.3389/fcimb.2017.00258 | Anopheles gambiae | Review of REL2/Imd signaling; describes PGRP-LC as main Imd receptor and discusses extracellular short PGRPs' modulatory roles relevant to PGRP-S3 function. |
| pqac-00000003 | Meister S et al., 2009, Anopheles gambiae PGRPLC-Mediated Defense against Bacteria Modulates Infections with Malaria Parasites | PLoS Pathogens | https://doi.org/10.1371/journal.ppat.1000542 | Anopheles gambiae | Structural modeling and functional data for PGRP-LC and overview of the seven Anopheles PGRPs; explicitly mentions PGRP-S2 and S3 in comparative/functional contexts. |
| pqac-00000004 | Meister S, 2006, The Role of PGRP Proteins in Innate Immunity Pathways in the Malaria Vector Anopheles gambiae | ArXiv / thesis | https://doi.org/10.11588/heidok.00006571 | Anopheles gambiae | Contains experimental/method details and notes that PGRP-S2 and PGRP-S3 are highly similar and sometimes experimentally co-targeted; useful for methodology and expression profiling context. |
| pqac-00000005 | Mendes C et al., 2010, Molecular evolution of the three short PGRPs of the malaria vectors Anopheles gambiae and Anopheles arabiensis in East Africa | BMC Evolutionary Biology | https://doi.org/10.1186/1471-2148-10-9 | Anopheles gambiae, Anopheles arabiensis | Population-genetics and evolutionary analysis showing PGRP-S2/S3 purifying selection, high haplotype diversity for PGRP-S3, and structural inference (amidase-related signatures) informing catalytic predictions. |

Table: A compact table of primary/contextual sources (context IDs) used to evaluate PGRP-S3 (UniProt D2STP8) in Anopheles gambiae, listing bibliographic details, URLs/DOIs, organism focus, and each source's specific relevance to PGRP-S3's function and signaling roles.

Limitations and recommendations
- Direct experimental characterization of An. gambiae PGRP-S3’s catalytic activity, substrate specificity (DAP vs Lys PGN), and tissue localization was not located in the present evidence set. Multiple functional studies co-silenced S2 and S3 due to sequence similarity, preventing S3-specific phenotypic attribution. Given domain predictions and conserved amidase signatures, PGRP-S3 is most likely a secreted Zn2+-amidase that hydrolyzes PGN to negatively regulate IMD signaling, but targeted in vitro enzymology and single-gene genetic dissection are needed to resolve S3-specific roles (meister2009anophelesgambiaepgrplcmediated pages 7-9, mendes2010molecularevolutionof pages 3-7, zakovic2017nfκblikesignalingpathway pages 2-4, audi2025apgrplc1rel2faxis pages 18-20).

Cited sources with links and dates
- Zakovic S, Levashina EA. NF-κB-Like Signaling Pathway REL2 in Immune Defenses of the Malaria Vector Anopheles gambiae. Frontiers in Cellular and Infection Microbiology. 2017-06-09. DOI: 10.3389/fcimb.2017.00258; URL: https://doi.org/10.3389/fcimb.2017.00258 (zakovic2017nfκblikesignalingpathway pages 2-4).
- Meister S, Agianian B, Turlure F, et al. Anopheles gambiae PGRPLC-Mediated Defense against Bacteria Modulates Infections with Malaria Parasites. PLoS Pathogens. 2009-08-28. DOI: 10.1371/journal.ppat.1000542; URL: https://doi.org/10.1371/journal.ppat.1000542 (meister2009anophelesgambiaepgrplcmediated pages 7-9).
- Mendes C, Felix R, Sousa A-M, et al. Molecular evolution of the three short PGRPs of the malaria vectors Anopheles gambiae and Anopheles arabiensis in East Africa. BMC Evolutionary Biology. 2010-01-07. DOI: 10.1186/1471-2148-10-9; URL: https://doi.org/10.1186/1471-2148-10-9 (mendes2010molecularevolutionof pages 3-7).
- Audi A, Zeineddine S, Jaber S, Osta MA. A PGRPLC1/Rel2-F axis controls Anopheles gambiae resistance to systemic infections with Gram-positive bacteria containing Lys-type peptidoglycan. PLOS Pathogens. 2025-09-19. DOI: 10.1371/journal.ppat.1013527; URL: https://doi.org/10.1371/journal.ppat.1013527 (background context on PGRP/REL2 modules and predicted amidase signatures for short PGRPs) (audi2025apgrplc1rel2faxis pages 18-20).
- El Moussawi LH. Functional and molecular characterization of the serine protease homologue CLIPA28 in the melanization response of Anopheles gambiae mosquitoes. 2019. (General insect PGRP background; no DOI provided in context) (moussawi2019functionalandmolecular pages 24-28).
- Meister S. The Role of PGRP Proteins in Innate Immunity Pathways in the Malaria Vector Anopheles gambiae. 2006. DOI: 10.11588/heidok.00006571; URL: https://doi.org/10.11588/heidok.00006571 (methodological and paralog-similarity context) (meister2006theroleof pages 69-74).

Summary conclusion
- Based on conserved domain architecture, evolutionary constraints, and pathway context in Anopheles, PGRP-S3 (UniProt D2STP8) is best annotated as a secreted, Zn2+-dependent PGN amidase that modulates IMD/REL2 signaling by degrading muropeptide ligands. Although S3-specific phenotypes remain insufficiently isolated from S2 in published functional studies, the combined genetic, evolutionary, and pathway evidence supports a role for PGRP-S3 in extracellular immune modulation that indirectly influences antibacterial defense and malaria parasite interactions via effects on microbiota-driven IMD signaling (mendes2010molecularevolutionof pages 3-7, zakovic2017nfκblikesignalingpathway pages 2-4, meister2009anophelesgambiaepgrplcmediated pages 7-9, audi2025apgrplc1rel2faxis pages 18-20, moussawi2019functionalandmolecular pages 24-28, meister2006theroleof pages 69-74).

References

1. (meister2009anophelesgambiaepgrplcmediated pages 7-9): Stephan Meister, Bogos Agianian, Fanny Turlure, Angela Relógio, Isabelle Morlais, Fotis C. Kafatos, and George K. Christophides. Anopheles gambiae pgrplc-mediated defense against bacteria modulates infections with malaria parasites. PLoS Pathogens, 5:e1000542, Aug 2009. URL: https://doi.org/10.1371/journal.ppat.1000542, doi:10.1371/journal.ppat.1000542. This article has 290 citations and is from a highest quality peer-reviewed journal.

2. (mendes2010molecularevolutionof pages 3-7): Cristina Mendes, Rute Felix, Ana-Margarida Sousa, Joana Lamego, Derek Charlwood, Virgílio E do Rosário, João Pinto, and Henrique Silveira. Molecular evolution of the three short pgrps of the malaria vectors anopheles gambiae and anopheles arabiensis in east africa. BMC Evolutionary Biology, 10:9-9, Jan 2010. URL: https://doi.org/10.1186/1471-2148-10-9, doi:10.1186/1471-2148-10-9. This article has 17 citations and is from a domain leading peer-reviewed journal.

3. (zakovic2017nfκblikesignalingpathway pages 2-4): Suzana Zakovic and Elena A. Levashina. Nf-κb-like signaling pathway rel2 in immune defenses of the malaria vector anopheles gambiae. Frontiers in Cellular and Infection Microbiology, Jun 2017. URL: https://doi.org/10.3389/fcimb.2017.00258, doi:10.3389/fcimb.2017.00258. This article has 36 citations and is from a poor quality or predatory journal.

4. (audi2025apgrplc1rel2faxis pages 18-20): Amani Audi, Suheir Zeineddine, Sana Jaber, and Mike A. Osta. A pgrplc1/rel2-f axis controls anopheles gambiae resistance to systemic infections with gram-positive bacteria containing lys-type peptidoglycan. PLOS Pathogens, 21:e1013527, Sep 2025. URL: https://doi.org/10.1371/journal.ppat.1013527, doi:10.1371/journal.ppat.1013527. This article has 0 citations and is from a highest quality peer-reviewed journal.

5. (moussawi2019functionalandmolecular pages 24-28): LH El Moussawi. Functional and molecular characterization of the serine protease homologue clipa28 in the melanization response of anopheles gambiae mosquitoes. Unknown journal, 2019.

6. (meister2006theroleof pages 69-74): Stephan Meister. The role of pgrp proteins in innate immunity pathways in the malaria vector anopheles gambiae. ArXiv, Jan 2006. URL: https://doi.org/10.11588/heidok.00006571, doi:10.11588/heidok.00006571. This article has 4 citations.

Citations

1. mendes2010molecularevolutionof pages 3-7
2. meister2009anophelesgambiaepgrplcmediated pages 7-9
3. moussawi2019functionalandmolecular pages 24-28
4. meister2006theroleof pages 69-74
5. https://doi.org/10.1371/journal.ppat.1013527
6. https://doi.org/10.3389/fcimb.2017.00258
7. https://doi.org/10.1371/journal.ppat.1000542
8. https://doi.org/10.11588/heidok.00006571
9. https://doi.org/10.1186/1471-2148-10-9
10. https://doi.org/10.1371/journal.ppat.1000542,
11. https://doi.org/10.1186/1471-2148-10-9,
12. https://doi.org/10.3389/fcimb.2017.00258,
13. https://doi.org/10.1371/journal.ppat.1013527,
14. https://doi.org/10.11588/heidok.00006571,