Evidence map›Paper›PMID 40058531›Full record

ArticleInsect biochemistry and molecular biology2025

Pattern recognition, hemolymph protease-14 activation, and enhancement of lysozyme-mediated bacteria killing by soluble peptidoglycan recognition proteins in Manduca sexta.

Chunxiang Hou, Yang Wang, Chao Xiong, Udeshika Kariyawasam, Tisheng Shan, Michael R Kanost, Haobo Jiang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Insect biochemistry and molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Chunxiang HouDepartment of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK, 74078, USA.
Yang WangDepartment of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK, 74078, USA.
Chao XiongDepartment of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK, 74078, USA.
Udeshika KariyawasamDepartment of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK, 74078, USA.
Tisheng ShanDepartment of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK, 74078, USA.
Michael R KanostDepartment of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS, 66506, USA.
Haobo JiangDepartment of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK, 74078, USA. Electronic address: haobo.jiang@okstate.edu.

Funding

Initiation and Regulation of Prophenoloxidase ActivationR01GM058634 · NIGMS · OKLAHOMA STATE UNIVERSITY STILLWATER · PI JIANG, HAOBO · 1999 to 2022
$4.0M
Function of hemolymph plasma proteins in insect immune responses (Equipment Supplement)R35GM141859 · NIGMS · KANSAS STATE UNIVERSITY · PI KANOST, MICHAEL R · 2021 to 2025
$2.0M
The immune serine protease pathways in Anopheles gambiaeR21AI180325 · NIAID · OKLAHOMA STATE UNIVERSITY STILLWATER · PI JIANG, HAOBO · 2024 to 2025
$409k
NIAID NIH HHS R21 AI180325NIGMS NIH HHS R01 GM058634NIGMS NIH HHS R35 GM141859
6 · The paper itself

Abstract

Peptidoglycan recognition proteins (PGRPs) detect invading bacteria during insect immune responses, and some can damage bacterial cell walls. We previously produced M. sexta PGRPs 1-5, 12, and 13, and demonstrated that the PGRP repertoire in hemolymph preferentially detects meso-diaminopimelic acid-peptidoglycans (DAP-PGs). In this study, we found that adding DAP-PGs and PGRPs to larval hemolymph significantly enhanced prophenoloxidase activation beyond the sum of their individual effects. Lys-PG of Micrococcus luteus and PGRP4/5 also displayed the synergy, but Lys-PG of Staphyloccous aureus did not. Structural modeling and ligand docking supported the preferrential binding of DAP-PGs over Lys-PGs. DAP/Lys-PG, PGRP3s/3f/5/13N, and microbe binding protein activated hemolymph protease-14 (HP14), suggesting that these PGRPs initiate the serine protease system in the same way as PGRP1. Using fluorescein-labeled M. luteus peptidoglycan as a substrate, we detected increases in fluorescence signal caused by PGRP2, 4, 13N, 12e, and 3f, suggesting that these PGRPs have amidase activity for hydrolyzing peptidoglycan, which was enhanced by Zn

Indexed as

Carrier ProteinsInsect ProteinsManducaMuramidaseAnimalsCatechol OxidaseEnzyme PrecursorsHemolymphLarvaMicrococcus luteusPeptidoglycanReceptors, Pattern RecognitionStaphylococcus aureusCarrier ProteinsCatechol OxidaseEnzyme PrecursorsInsect ProteinsMuramidasePeptidoglycanpeptidoglycan recognition proteinpro-phenoloxidaseReceptors, Pattern RecognitionHemolymph proteinInsect immunityMelanizationPattern recognitionSerine protease cascade

Identifiers

PMID40058531
PMCPMC12066225

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.