Evidence map›Paper›PMID 27307559›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2016

An Inhibitor of the Alternative Pathway of Complement in Saliva of New World Anopheline Mosquitoes.

Antonio F Mendes-Sousa, Daniel C Queiroz, Vladimir F Vale, José M C Ribeiro, Jesus G Valenzuela, Nelder F Gontijo, John F Andersen

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 23% of its field
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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Yersinia pestis ΔApplied and environmental microbiology · 2023
    Article
  3. Review
  4. Article
  5. Article
  6. Arboviruses: How Saliva Impacts the Journey from Vector to Host.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Frontiers in cellular and infection microbiology · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

7 authors at 2 institutions in 2 countries.

Antonio F Mendes-SousaLaboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, MD 20852; Department of Parasitology, University of Minas Gerais, Belo Horizonte, Minas Gerais 30123-970, Brazil; and.ORCID 0000-0002-2019-1348
Daniel C QueirozDepartment of Parasitology, University of Minas Gerais, Belo Horizonte, Minas Gerais 30123-970, Brazil; and.ORCID 0000-0002-6607-8818
Vladimir F ValeDepartment of Parasitology, University of Minas Gerais, Belo Horizonte, Minas Gerais 30123-970, Brazil; and Laboratory of Simuliids and Onchocerciasis, Oswaldo Cruz Institute, Fiocruz, Rio de Janeiro 21040-900, Brazil.ORCID 0000-0002-6505-5999
José M C RibeiroLaboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, MD 20852;
Jesus G ValenzuelaLaboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, MD 20852;
Nelder F GontijoDepartment of Parasitology, University of Minas Gerais, Belo Horizonte, Minas Gerais 30123-970, Brazil; and.ORCID 0000-0003-3357-2497
John F AndersenLaboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, MD 20852; jandersen@niaid.nih.gov.
Universidade Federal de Minas Gerais · BRNational Institutes of Health · US

Funding

Molecular approaches to understand vector-host and vector-pathogen interactionsZIAAI000932 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI VALENZUELA, JESUS · 2009 to 2025
$23.1M
Vector-Borne Diseases: Biology Of Vector Host RelationshipZIAAI000810 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI RIBEIRO, JOSE · 2009 to 2025
$20.8M
Vector-Borne Diseases: Molecular Mechanisms in Vector-Host InteractionsZIAAI001012 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI RIBEIRO, JOSE · 2009 to 2025
$9.4M
Vector-Borne Diseases: Molecular Mechanisms in Vector-Host InteractionsZ01AI001012 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI RIBEIRO, JOSE · 2007 to 2008
$1.5M
Intramural NIH HHS Z01 AI001012Intramural NIH HHS Z99 AI999999
6 · The paper itself

Abstract

The complement system present in circulating blood is an effective mechanism of host defense, responsible for the killing of pathogens and the production of potent anaphylatoxins. Inhibitors of the complement system have been described in the saliva of hematophagous arthropods that are involved in the protection of digestive tissues against complement system-mediated damage. In this study, we describe albicin, a novel inhibitor of the alternative pathway of complement from the salivary glands of the malaria vector, Anopheles albimanus The inhibitor was purified from salivary gland homogenates by reverse-phase HPLC and identified by mass spectrometry as a small (13.4-kDa) protein related to the gSG7 protein of Anopheles gambiae and Anopheles stephensi Recombinant albicin was produced in Escherichia coli and found to potently inhibit lysis of rabbit erythrocytes in assays of the alternative pathway while having no inhibitory effect on the classical or lectin pathways. Albicin also inhibited the deposition of complement components on agarose-coated plates, although it could not remove previously bound components. Antisera produced against recombinant albicin recognized both the native and recombinant inhibitors and also blocked their activities in in vitro assays. Using surface plasmon resonance and enzymatic assays, we found that albicin binds and stabilizes the C3-convertase complex (C3bBb) formed on a properdin surface and inhibits the convertase activity of a reconstituted C3bBb complex in solution. The data indicate that albicin specifically recognizes the activated form of the complex, allowing more efficient inhibition by an inhibitor whose quantity is limited.

Indexed as

AnimalsAnophelesBlotting, WesternChromatography, High Pressure LiquidComplement Pathway, AlternativeEnzyme-Linked Immunosorbent AssayFemaleInsect ProteinsMass SpectrometryPolymerase Chain ReactionRabbitsSalivaSalivary Proteins and PeptidesSurface Plasmon Resonancealbicin protein, Anopheles albimanusInsect ProteinsSalivary Proteins and Peptides

Identifiers

PMID27307559
PMCPMC4989506
OpenAlexW2425292213

What OpenQuestion holds

Textmetadata
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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.