Evidence map›Paper›PMID 39799989›Full record

ArticleInsect biochemistry and molecular biology2025

CLIPA protein pairs function as cofactors for prophenoloxidase activation in Anopheles gambiae.

Yang Wang, Qiao Jin, Michael R Kanost, Haobo Jiang

Abstract read
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. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Partial reconstitution of the prophenoloxidase activation system inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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

4 authors.

Yang WangDepartment of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK, 74078, USA.
Qiao JinDepartment 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

Insect prophenoloxidases (proPO) are activated during immune responses by a proPO activating protease (PAP) in the presence of a high molecular weight cofactor assembled from serine protease homologs (SPH) that lack proteolytic activity. PAPs and the SPHs have a similar architecture, with an amino-terminal clip domain and a carboxyl-terminal protease domain. The SPHs belong to CLIPA subfamily of SP-related proteins. In Manduca sexta, a well characterized biochemical model system for insect immunity, the functional SPH cofactor contains one molecule each from two SPH subfamilies, SPH-I and SPH-II. In Anopheles gambiae, three SPHI-SPHII pairs (CLIPs A4-A6, A4-A7Δ, and A4-A12) were previously reported as cofactors for CLIPB9-mediated activation of proPO2 and proPO7. In this study, we produced recombinant proteins for two splicing variants of CLIPA7, proCLIPA7s (s for short), proCLIPA7f (f for full-length) and proCLIPA14. We cleaved each along with proCLIPA4 using M. sexta PAP3 and found that the CLIPA pairs A4-A7s and A4-A14 are better than A4-A7f in generating highly active PO2 or PO7. CLIPA7f and CLIPA7s, products of alternative splicing, have different strengths as cofactors in combination with CLIPA4. Because mRNA for CLIPA7f is expressed at a significantly higher level than CLIPA7s, cofactors with the weaker combination A4-A7f may predominate in hemolymph, resulting in a potential dampening effect on proPO activation as a regulatory mechanism for altering the strength of the melanization response. A. gambiae CLIPB10x

Indexed as

AnophelesCatechol OxidaseEnzyme PrecursorsInsect ProteinsSerine EndopeptidasesAnimalsCoenzymesCatechol OxidaseCoenzymesEnzyme PrecursorsInsect Proteinspro-phenoloxidaseSerine EndopeptidasesClip domainHemolymph proteinInsect immunityMelanizationProtease cascadeSerine protease homolog

Identifiers

PMID39799989
PMCPMC11807748

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.