Evidence map›Paper›PMID 27165123›Full record

ArticleParasites & vectors2016

An antibody against an Anopheles albimanus midgut myosin reduces Plasmodium berghei oocyst development.

Alba N Lecona-Valera, Dingyin Tao, Mario H Rodríguez, Tomás López, Rhoel R Dinglasan, María C Rodríguez

Open access · goldAbstract read
In one paragraph

Article in Parasites & vectors, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Transcriptome analysis ofCurrent research in parasitology & vector-borne diseases · 2025
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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

6 authors at 2 institutions in 2 countries.

Alba N Lecona-ValeraCenter of Research on Infectious Diseases, National Institute of Public Health, Av. Universidad 655, Col. Santa María Ahuacatitlán, Cuernavaca, Morelos, C. P. 62508, Mexico.
Dingyin TaoW. Harry Feinstone Department of Molecular Microbiology & Immunology and the Malaria Research Institute, Johns Hopkins Bloomberg School of Public Health, 615 North Wolfe Street, Baltimore, Maryland, 21205, USA.
Mario H RodríguezCenter of Research on Infectious Diseases, National Institute of Public Health, Av. Universidad 655, Col. Santa María Ahuacatitlán, Cuernavaca, Morelos, C. P. 62508, Mexico.
Tomás LópezInstituto de Biotecnología, Universidad Nacional Autónoma de Méxic006F, Av. Universidad 2001, Colonia Chamilpa, Cuernavaca, Morelos, 62210, Mexico.
Rhoel R DinglasanW. Harry Feinstone Department of Molecular Microbiology & Immunology and the Malaria Research Institute, Johns Hopkins Bloomberg School of Public Health, 615 North Wolfe Street, Baltimore, Maryland, 21205, USA.
María C RodríguezCenter of Research on Infectious Diseases, National Institute of Public Health, Av. Universidad 655, Col. Santa María Ahuacatitlán, Cuernavaca, Morelos, C. P. 62508, Mexico. mrodri@insp.mx.
Instituto Nacional de Salud Pública · MXJohns Hopkins University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMalaria parasites are transmitted by Anopheles mosquitoes. Although several studies have identified mosquito midgut surface proteins that are putatively important for Plasmodium ookinete invasion, only a few have characterized these protein targets and demonstrated transmission-blocking activity. Molecular information about these proteins is essential for the development of transmission-blocking vaccines (TBV). The aim of the present study was to test three monoclonal antibodies (mAbs), A-140, A-78 and A-10, for their ability to recognize antigens and block oocyst infection of the midgut of Anopheles albimanus, a major malaria vector in Latin America.

methodWestern-blot of mAbs on antigens from midgut brush border membrane vesicles was used to select antibodies. Three mAbs were tested by membrane feeding assays to evaluate their potential transmission-blocking activity against Plasmodium berghei. The cognate antigens recognized by mAbs with oocyst-reducing activity were determined by immunoprecipitation followed by liquid chromatography tandem mass spectrometry.

resultsOnly one mAb, A-140, significantly reduced oocyst infection intensity. Hence, its probable protein target in the Anopheles albimanus midgut was identified and characterized. It recognized three high-molecular mass proteins from a midgut brush border microvilli vesicle preparation. Chemical deglycosylation assays confirmed the peptide nature of the epitope recognized by mAb A-140. Immunoprecipitation followed by proteomic identification with tandem mass spectrometry revealed five proteins, presumably extracted together as a complex. Of these, AALB007909 had the highest mascot score and corresponds to a protein with a myosin head motor domain, indicating that the target of mAb A-140 is probably myosin located on the microvilli of the mosquito midgut.

conclusionThese results provide support for the participation of myosin in mosquito midgut invasion by Plasmodium ookinetes. The potential inclusion of this protein in the design of new multivalent vaccine strategies for blocking Plasmodium transmission is discussed.

Indexed as

AnimalsAnophelesAntibodies, MonoclonalDigestive SystemFemaleInsect VectorsMalariaMyosinsOocystsPlasmodium bergheiProteomicsAntibodies, MonoclonalMyosinsAnopheles albimanusMidgutMonoclonal antibodyMyosinPlasmodium berghei

Identifiers

PMID27165123
PMCPMC4863318
OpenAlexW2358142623

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.