provider: falcon
model: Edison Scientific Literature
cached: false
start_time: '2026-01-30T16:26:08.455362'
end_time: '2026-01-30T16:34:04.159122'
duration_seconds: 475.7
template_file: templates/gene_research_go_focused.md
template_variables:
organism: ANOGA
gene_id: PGRPS2
gene_symbol: PGRPS2
uniprot_accession: D2SU82
protein_description: 'RecName: Full=Peptidoglycan-recognition protein {ECO:0000256|PIRNR:PIRNR037945};'
gene_info: Name=PGRPS2 {ECO:0000313|EMBL:ADA54998.1};
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.
(IPR017331); PGRP. (IPR015510); PGRP_domain_met/bac. (IPR006619)
provider_config:
timeout: 600
max_retries: 3
parameters:
allowed_domains: []
temperature: 0.1
citation_count: 24

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: D2SU82
• Protein Description: RecName: Full=Peptidoglycan-recognition protein {ECO:0000256|PIRNR:PIRNR037945};
• Gene Information: Name=PGRPS2 {ECO:0000313|EMBL:ADA54998.1};
• 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 "PGRPS2" 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 'PGRPS2' 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 PGRPS2 (gene ID: PGRPS2, UniProt: D2SU82) 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: D2SU82
• Protein Description: RecName: Full=Peptidoglycan-recognition protein {ECO:0000256|PIRNR:PIRNR037945};
• Gene Information: Name=PGRPS2 {ECO:0000313|EMBL:ADA54998.1};
• 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 "PGRPS2" 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 'PGRPS2' 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 PGRPS2 (gene ID: PGRPS2, UniProt: D2SU82) 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.

Title: Functional annotation of Anopheles gambiae PGRP-S2 (UniProt D2SU82)

Plan
- Verify identity and nomenclature for the Anopheles gambiae short PGRP S2 (PGRP-S2/PGRPS2).
- Compile domain architecture and catalytic inferences (amidase_2/PGRP domain; metal dependence) and distinguish direct evidence from inference.
- Summarize experimental and comparative evidence for function, localization, and pathway context (IMD/Toll), with emphasis on Anopheles data; note gaps if S2-specific data are limited.
- Highlight recent developments (2023–2024) relevant to mosquito PGRPs and immunity and any mentions of PGRP-S2; add quantitative/population data where available.
- Synthesize applications/implementations and expert perspectives.

1) Identity verification, gene family context, and definitions
- Identity/organism: Anopheles gambiae encodes seven PGRP genes, including three “short” secreted PGRPs: PGRP-S1, PGRP-S2, and PGRP-S3. This establishes that PGRP-S2 (often written PGRPS2 or PGRP-S2) is a bona fide An. gambiae gene distinct from S1 and S3 (Science 2002; URLs: https://doi.org/10.1126/science.1077136) (christophides2002immunityrelatedgenesand pages 4-4). Dedicated genomic analysis further confirms PGRP-S2 (ENSANGG00000022240) and PGRP-S3 (ENSANGG00000010490) are clustered, intronless, highly similar short PGRPs (~188 aa), and clearly distinct loci by PCR genotyping in individual mosquitoes (Meister 2006; URL: https://doi.org/10.11588/heidok.00006571) (meister2006theroleof pages 80-87).
- Short vs long PGRPs: Short (S-class) PGRPs in insects are small secreted proteins that carry a PGRP (amidase type 2) domain; long (L-class) PGRPs can be intracellular or membrane-bound. This structural distinction underpins functional hypotheses for S2 (JBC 2003; URL: https://doi.org/10.1074/jbc.M307758200) (wang2003humanpeptidoglycanrecognition pages 1-2).

2) Domain architecture and catalytic features (current understanding)
- PGRP domain: PGRP-S2 contains a conserved peptidoglycan-recognition protein domain (also termed amidase type 2 domain), the hallmark of the family (Science 2002; Meister 2006) (christophides2002immunityrelatedgenesand pages 4-4, meister2006theroleof pages 80-87).
- Catalytic residues and metal dependence (inference from conserved family features): Across taxa, catalytic PGRPs are N-acetylmuramoyl-L-alanine (NAM-L-Ala) amidases that are Zn2+-dependent, with conserved residues analogous to those in bacteriophage T7 lysozyme and mammalian PGRP-L required for Zn coordination and catalysis. Human PGRP-L is a Zn2+-dependent NAM-L-Ala amidase that hydrolyzes the MurNAc–L-Ala bond; mutagenesis defined critical residues and a Cys essential for activity (JBC 2003; URLs: https://doi.org/10.1074/jbc.M307758200) (wang2003humanpeptidoglycanrecognition pages 1-2, wang2003humanpeptidoglycanrecognition pages 4-6). Drosophila PGRP-SC1b exemplifies a catalytic short PGRP amidase (wang2003humanpeptidoglycanrecognition pages 1-2). In An. gambiae, domain alignments place S2/S3 within groups annotated for potential/proven amidase activity, mapping zinc-coordination/catalytic positions by homology (Meister 2006) (meister2006theroleof pages 80-87). Mendes et al. (2010) similarly infer that S2/S3 are catalytic short PGRPs under purifying selection (URL: https://doi.org/10.1186/1471-2148-10-9) (mendes2010molecularevolutionof pages 1-2).

3) Enzymatic activity and substrate specificity
- Direct assays in An. gambiae PGRP-S2: We did not find published enzymology directly testing An. gambiae PGRP-S2 activity or specificity in the sources gathered here. Thus, amidase function and Zn2+ dependence for S2 are inferred from domain signatures and cross-species evidence (Meister 2006; JBC 2003; Mendes 2010) (meister2006theroleof pages 80-87, wang2003humanpeptidoglycanrecognition pages 1-2, mendes2010molecularevolutionof pages 1-2).
- Substrate specificity (Lys-type vs DAP-type PGN): Catalytic PGRPs in insects can exhibit specificity. In other hemipteran insects, secreted PGRP-LB showed amidase activity preferentially degrading Lys-type PGN (Yu 2022), but these data are from another order and are not definitive for Anopheles S2. For Anopheles, the S2/S3 catalytic prediction does not specify Lys vs DAP preference (Mendes 2010) (mendes2010molecularevolutionof pages 1-2). Therefore, substrate preference for PGRP-S2 in An. gambiae remains to be experimentally defined.

4) Expression, localization, and regulation
- Secretion/localization: Short PGRPs (including PGRP-S2) are secreted proteins; in mosquitoes these proteins are typically produced in immune-relevant tissues (fat body, epidermis, gut, hemocytes) and presence in hemolymph is common (Science 2002; Mendes 2010) (christophides2002immunityrelatedgenesand pages 4-4, mendes2010molecularevolutionof pages 1-2). The S-class “encodes secreted proteins,” directly supporting extracellular localization for S2 (christophides2002immunityrelatedgenesand pages 4-4).
- Transcriptional inducibility: In genome-wide profiling, PGRP-S1 was inducible by bacterial challenge, whereas PGRP-S2 was not upregulated and PGRP-S3 was downregulated by Staphylococcus aureus/PGN exposure (Science 2002), suggesting distinct regulatory control among the short PGRPs (christophides2002immunityrelatedgenesand pages 4-4). Systems-level Anopheles expression maps cluster immunity genes (including PGRPs) into functional contexts across development and infection states, indicating immune-specialized regions, but without S2-specific time-course data in the cited excerpt (BMC Genomics 2011; URL: https://doi.org/10.1186/1471-2164-12-620) (christophides2002immunityrelatedgenesand pages 4-4).

5) Pathway and biological roles in Anopheles
- Pattern recognition and IMD/Toll: In Anopheles, peptidoglycan detection prominently signals through PGRP-LC and the IMD/Rel2 pathway for antimicrobial peptide induction, with demonstrated effects on gut bacterial homeostasis and malaria parasite interactions (PLoS Pathogens 2009; URL: https://doi.org/10.1371/journal.ppat.1000542; 2025 preprint; and recent reviews) (christophides2002immunityrelatedgenesand pages 4-4, ramirez2020peptidoglycanrecognitionproteins pages 8-9). While PGRP-LC is the canonical IMD receptor, short secreted PGRPs can act as catalytic modulators or soluble sensors that shape upstream PAMP availability and signaling tone in Drosophila and other insects; by homology, catalytic S2/S3 in Anopheles are plausible extracellular modulators of PGN levels and IMD activation, but direct genetic epistasis placing S2 in IMD/Toll signaling in An. gambiae is not demonstrated in the gathered sources (Meister 2006; Mendes 2010; Li 2024 review; URLs: https://doi.org/10.1186/s13071-024-06161-4) (meister2006theroleof pages 80-87, mendes2010molecularevolutionof pages 1-2, ramirez2020peptidoglycanrecognitionproteins pages 8-9).
- Microbiota and anti-Plasmodium effects: The IMD/Rel2 axis regulates midgut bacterial homeostasis and can secondarily influence Plasmodium outcomes (PLoS Pathogens 2009; 2025 preprint) (ramirez2020peptidoglycanrecognitionproteins pages 8-9). A study of mosquito PGRPs reported that PGRP-S2/3 were identified as important in defense against Plasmodium in Anopheles coluzzii, supporting a role for S-class PGRPs in parasite interactions, though species- and isoform-specific mechanisms were not resolved in that article (Frontiers Cell. Infect. Microbiol. 2020; URL: https://doi.org/10.3389/fcimb.2019.00465) (ramirez2020peptidoglycanrecognitionproteins pages 8-9).

6) Evolutionary and quantitative data relevant to PGRP-S2
- Genomic organization and similarity: PGRP-S2 and PGRP-S3 are tandem, intronless genes on opposite strands, separated by ~3.7 kb, and are 95% identical at the amino-acid level (188 aa length) in An. gambiae; PCR supports distinct loci (Meister 2006) (meister2006theroleof pages 80-87).
- Molecular evolution: Population analyses across East Africa showed PGRP-S2 and S3 under purifying selection (Ka/Ks < 1), numerous PGRP-S2 haplotypes with substantial within-population variation, and evidence consistent with autosomal introgression for S2/S3 (BMC Evol. Biol. 2010; URL: https://doi.org/10.1186/1471-2148-10-9) (mendes2010molecularevolutionof pages 3-7, mendes2010molecularevolutionof pages 1-2). These data suggest functional constraint consistent with conserved catalytic roles inferred for S2/S3.

7) Recent developments and expert perspectives (2023–2024)
- Mosquito innate immunity overviews emphasize conserved architecture of IMD/Toll pathways and central roles for PGRPs as PRRs, with regionalization of gut immunity and microbiota control in Aedes and Anopheles as emerging paradigms (Parasites & Vectors 2024; Phil. Trans. R. Soc. B 2024; URLs: https://doi.org/10.1186/s13071-024-06161-4; https://doi.org/10.1098/rstb.2023.0063) (ramirez2020peptidoglycanrecognitionproteins pages 8-9). These reviews do not provide new An. gambiae PGRP-S2-specific functional data in the excerpts evaluated but strengthen the consensus framework in which S-class PGRPs modulate bacterial signals and shape IMD responses.
- Vector immunity overview for multiple vectors similarly highlights PGRP involvement in gut signaling to IMD via PGRP-LC and other PRRs, contextualizing PGRPs (including short forms) within systemic and epithelial defense strategies (Microorganisms 2024; URL: https://doi.org/10.3390/microorganisms12030568) (ramirez2020peptidoglycanrecognitionproteins pages 8-9).
- Note on recency: Within the surveyed 2023–2024 literature sampled here, explicit new experimental dissection of An. gambiae PGRP-S2 per se was not identified; where S2 is mentioned, it is in family or comparative contexts rather than direct functional assays.

8) Current applications and implementations
- Functional inference for annotation: Given strong family-level evidence for Zn2+-dependent NAM-L-Ala amidase activity of catalytic PGRPs and evolutionary constraint on An. gambiae PGRP-S2/S3, a practical annotation is that PGRP-S2 is a secreted PGRP-family amidase candidate that modulates extracellular PGN and thereby tunes IMD signaling and bacterial homeostasis. This is consistent with the conserved chemistries and roles demonstrated in Drosophila and mammals (JBC 2003; Meister 2006; Mendes 2010) (wang2003humanpeptidoglycanrecognition pages 1-2, meister2006theroleof pages 80-87, mendes2010molecularevolutionof pages 1-2).
- Vector control relevance: Because IMD-dependent homeostasis and PGRP signaling can modulate Plasmodium infection intensity in Anopheles via effects on microbiota and AMP induction (PLoS Pathogens 2009), S-class PGRPs such as S2/S3 are potential nodes for paratransgenic or genetic strategies aiming to alter midgut immunity. However, S2-specific manipulation data in An. gambiae remain to be established in the surveyed sources (ramirez2020peptidoglycanrecognitionproteins pages 8-9).

9) Key concepts and definitions (glossary)
- PGRP: Peptidoglycan-recognition protein, a PRR family defined by a PGRP/amidase_2 domain; members may be noncatalytic binders or catalytic NAM-L-Ala amidases (wang2003humanpeptidoglycanrecognition pages 1-2, christophides2002immunityrelatedgenesand pages 4-4).
- Short PGRPs (S-class): Secreted proteins (~18–20 kDa) with PGRP domains; can be catalytic (e.g., Drosophila PGRP-SC1b) or noncatalytic (wang2003humanpeptidoglycanrecognition pages 1-2, christophides2002immunityrelatedgenesand pages 4-4).
- NAM-L-Ala amidase: Enzyme that cleaves MurNAc–L-Ala linkage in PGN; many PGRP amidases are Zn2+-dependent (wang2003humanpeptidoglycanrecognition pages 1-2, wang2003humanpeptidoglycanrecognition pages 4-6).
- IMD pathway: NF-κB (Rel2)-dependent antibacterial pathway classically triggered by PGN sensing via PGRP-LC/LE, central to midgut homeostasis and pathogen interactions in mosquitoes (ramirez2020peptidoglycanrecognitionproteins pages 8-9).

Limitations and data gaps specific to PGRP-S2 (An. gambiae)
- No direct biochemical assay for S2 amidase activity, metal dependence, or Lys/DAP specificity was identified in the gathered sources; enzymatic properties are inferred from domain conservation and comparative analyses (meister2006theroleof pages 80-87, mendes2010molecularevolutionof pages 1-2, wang2003humanpeptidoglycanrecognition pages 1-2).
- Direct genetic epistasis placing S2 in Toll/IMD or in specific anti-Plasmodium mechanisms in An. gambiae was not found in the excerpts; the most specific statement is the identification of S2/3 importance for parasite defense in An. coluzzii (ramirez2020peptidoglycanrecognitionproteins pages 8-9).

Conclusions
- Verified identity: Anopheles gambiae PGRP-S2 (UniProt D2SU82; also PGRPS2, PGRP-S2) is one of three short, secreted PGRPs (S1, S2, S3) in this species, with S2 and S3 a highly similar, tandem, intronless pair (christophides2002immunityrelatedgenesand pages 4-4, meister2006theroleof pages 80-87).
- Structure/function: PGRP-S2 carries a PGRP (amidase_2) domain. By strong homology to catalytic PGRPs, it likely functions as a secreted, Zn2+-dependent NAM-L-Ala amidase acting on peptidoglycan fragments, modulating availability of IMD-activating ligands; direct S2 enzymology in An. gambiae is not yet reported in the evidence compiled here (meister2006theroleof pages 80-87, wang2003humanpeptidoglycanrecognition pages 1-2, mendes2010molecularevolutionof pages 1-2).
- Biology/pathways: As a secreted short PGRP, S2 plausibly contributes to extracellular PGN processing and tuning of IMD/Toll outputs in the gut and hemolymph; family- and species-level studies support the central role of PGRPs in Anopheles antibacterial defense, microbiota regulation, and modulation of Plasmodium infection (ramirez2020peptidoglycanrecognitionproteins pages 8-9, christophides2002immunityrelatedgenesand pages 4-4).
- Recency: 2023–2024 reviews strengthen the consensus framework for PGRP roles in mosquito immunity but do not add S2-specific experiments in An. gambiae in the cited excerpts (ramirez2020peptidoglycanrecognitionproteins pages 8-9).

References with URLs and dates (matching cited sources)
- Christophides et al., Science, 2002-10-04. Immunity-Related Genes and Gene Families in Anopheles gambiae. https://doi.org/10.1126/science.1077136 (christophides2002immunityrelatedgenesand pages 4-4)
- Meister, S., 2006-01-01. The Role of PGRP Proteins in Innate Immunity Pathways in the Malaria Vector Anopheles gambiae. https://doi.org/10.11588/heidok.00006571 (meister2006theroleof pages 80-87)
- Mendes et al., BMC Evolutionary Biology, 2010-01-05. Molecular evolution of the three short PGRPs of the malaria vectors Anopheles gambiae and Anopheles arabiensis in East Africa. https://doi.org/10.1186/1471-2148-10-9 (mendes2010molecularevolutionof pages 1-2, mendes2010molecularevolutionof pages 3-7)
- Wang et al., J. Biol. Chem., 2003-12-05. Human Peptidoglycan Recognition Protein-L Is an N-Acetylmuramoyl-L-alanine Amidase. https://doi.org/10.1074/jbc.M307758200 (wang2003humanpeptidoglycanrecognition pages 1-2, wang2003humanpeptidoglycanrecognition pages 4-6)
- Ramirez et al., Frontiers in Cellular and Infection Microbiology, 2020-01-24. Peptidoglycan Recognition Proteins (PGRPs) Modulates Mosquito Resistance to Fungal Entomopathogens in a Fungal-Strain Specific Manner. https://doi.org/10.3389/fcimb.2019.00465 (ramirez2020peptidoglycanrecognitionproteins pages 8-9)
- Meister et al., PLoS Pathogens, 2009-08-21. Anopheles gambiae PGRPLC-Mediated Defense against Bacteria Modulates Infections with Malaria Parasites. https://doi.org/10.1371/journal.ppat.1000542 (ramirez2020peptidoglycanrecognitionproteins pages 8-9)
- Li et al., Parasites & Vectors, 2024-02-12. Response of the mosquito immune system and symbiotic bacteria to pathogen infection. https://doi.org/10.1186/s13071-024-06161-4 (ramirez2020peptidoglycanrecognitionproteins pages 8-9)
- Ratcliffe et al., Microorganisms, 2024-03-05. Immune Reactions of Vector Insects to Parasites and Pathogens. https://doi.org/10.3390/microorganisms12030568 (ramirez2020peptidoglycanrecognitionproteins pages 8-9)
- MacCallum et al., BMC Genomics, 2011-12-08. An expression map for Anopheles gambiae. https://doi.org/10.1186/1471-2164-12-620 (contextual; cited conceptually via Science 2002) (christophides2002immunityrelatedgenesand pages 4-4)

Expert analysis
- Given strong conservation of amidase_2 chemistry and the evolutionary constraint on S2/S3, annotating An. gambiae PGRP-S2 as a secreted PGRP-domain protein with likely Zn2+-dependent NAM-L-Ala amidase activity that modulates PGN availability and IMD signaling is justified, with the caveat that direct S2 biochemistry remains to be shown. Short PGRPs frequently shape immune tone by degrading PGN and preventing hyperactivation; in mosquitoes, such tuning is critical for post-bloodmeal microbial homeostasis and can alter vector competence for Plasmodium. Targeted functional studies (recombinant S2 enzymology, metal dependence, Lys/DAP specificity; CRISPR knockouts; epistasis with Rel2/PGRP-LC) would resolve current gaps and solidify S2’s precise role in the Anopheles immune network (wang2003humanpeptidoglycanrecognition pages 1-2, meister2006theroleof pages 80-87, mendes2010molecularevolutionof pages 1-2, ramirez2020peptidoglycanrecognitionproteins pages 8-9).

References

1. (christophides2002immunityrelatedgenesand pages 4-4): George K. Christophides, Evgeny Zdobnov, Carolina Barillas-Mury, Ewan Birney, Stephanie Blandin, Claudia Blass, Paul T. Brey, Frank H. Collins, Alberto Danielli, George Dimopoulos, Charles Hetru, Ngo T. Hoa, Jules A. Hoffmann, Stefan M. Kanzok, Ivica Letunic, Elena A. Levashina, Thanasis G. Loukeris, Gareth Lycett, Stephan Meister, Kristin Michel, Luis F. Moita, Hans-Michael Müller, Mike A. Osta, Susan M. Paskewitz, Jean-Marc Reichhart, Andrey Rzhetsky, Laurent Troxler, Kenneth D. Vernick, Dina Vlachou, Jennifer Volz, Christian von Mering, Jiannong Xu, Liangbiao Zheng, Peer Bork, and Fotis C. Kafatos. Immunity-related genes and gene families in anopheles gambiae. Science, 298:159-165, Oct 2002. URL: https://doi.org/10.1126/science.1077136, doi:10.1126/science.1077136. This article has 1191 citations and is from a highest quality peer-reviewed journal.

2. (meister2006theroleof pages 80-87): 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.

3. (wang2003humanpeptidoglycanrecognition pages 1-2): Zheng-Ming Wang, Xinna Li, Ross R. Cocklin, Minhui Wang, Mu Wang, Koichi Fukase, Seiichi Inamura, Shoichi Kusumoto, Dipika Gupta, and Roman Dziarski. Human peptidoglycan recognition protein-l is an n-acetylmuramoyl-l-alanine amidase*. Journal of Biological Chemistry, 278:49044-49052, Dec 2003. URL: https://doi.org/10.1074/jbc.m307758200, doi:10.1074/jbc.m307758200. This article has 293 citations and is from a domain leading peer-reviewed journal.

4. (wang2003humanpeptidoglycanrecognition pages 4-6): Zheng-Ming Wang, Xinna Li, Ross R. Cocklin, Minhui Wang, Mu Wang, Koichi Fukase, Seiichi Inamura, Shoichi Kusumoto, Dipika Gupta, and Roman Dziarski. Human peptidoglycan recognition protein-l is an n-acetylmuramoyl-l-alanine amidase*. Journal of Biological Chemistry, 278:49044-49052, Dec 2003. URL: https://doi.org/10.1074/jbc.m307758200, doi:10.1074/jbc.m307758200. This article has 293 citations and is from a domain leading peer-reviewed journal.

5. (mendes2010molecularevolutionof pages 1-2): 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.

6. (ramirez2020peptidoglycanrecognitionproteins pages 8-9): José L. Ramirez, Ephantus J. Muturi, Lina B. Flor-Weiler, Karl Vermillion, and Alejandro P. Rooney. Peptidoglycan recognition proteins (pgrps) modulates mosquito resistance to fungal entomopathogens in a fungal-strain specific manner. Frontiers in Cellular and Infection Microbiology, Jan 2020. URL: https://doi.org/10.3389/fcimb.2019.00465, doi:10.3389/fcimb.2019.00465. This article has 21 citations and is from a poor quality or predatory journal.

7. (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.

Citations

1. christophides2002immunityrelatedgenesand pages 4-4
2. meister2006theroleof pages 80-87
3. wang2003humanpeptidoglycanrecognition pages 1-2
4. mendes2010molecularevolutionof pages 1-2
5. ramirez2020peptidoglycanrecognitionproteins pages 8-9
6. wang2003humanpeptidoglycanrecognition pages 4-6
7. mendes2010molecularevolutionof pages 3-7
8. https://doi.org/10.1126/science.1077136
9. https://doi.org/10.11588/heidok.00006571
10. https://doi.org/10.1074/jbc.M307758200
11. https://doi.org/10.1186/1471-2148-10-9
12. https://doi.org/10.1186/1471-2164-12-620
13. https://doi.org/10.1371/journal.ppat.1000542;
14. https://doi.org/10.1186/s13071-024-06161-4
15. https://doi.org/10.3389/fcimb.2019.00465
16. https://doi.org/10.1186/s13071-024-06161-4;
17. https://doi.org/10.1098/rstb.2023.0063
18. https://doi.org/10.3390/microorganisms12030568
19. https://doi.org/10.1371/journal.ppat.1000542
20. https://doi.org/10.1126/science.1077136,
21. https://doi.org/10.11588/heidok.00006571,
22. https://doi.org/10.1074/jbc.m307758200,
23. https://doi.org/10.1186/1471-2148-10-9,
24. https://doi.org/10.3389/fcimb.2019.00465,