Evidence map›Paper›PMID 21905706›Full record

ArticleJournal of proteome research2011

Ookinete-interacting proteins on the microvillar surface are partitioned into detergent resistant membranes of Anopheles gambiae midguts.

Lindsay A Parish, David R Colquhoun, Ceereena Ubaida Mohien, Alexey E Lyashkov, David R Graham, Rhoel R Dinglasan

Abstract read
In one paragraph

Article in Journal of proteome research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Trial
  2. Review
  3. Croquemort-scavenger receptor class B 2 (Journal of biosciences · 2025
    Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Differential roles of an Anopheline midgut GPI-anchored protein in mediating Plasmodium falciparum and Plasmodium vivax ookinete invasion.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2014
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
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  20. Review
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.

Lindsay A ParishW. Harry Feinstone Department of Molecular Microbiology & Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD 21205, USA.
David R Colquhoun
Ceereena Ubaida Mohien
Alexey E Lyashkov
David R Graham
Rhoel R Dinglasan

Funding

Training: Molecular & Cellular Bases of Infectious DiseasesT32AI007417 · NIAID · JOHNS HOPKINS UNIVERSITY · PI Arturo Casadevall · 1994 to 2026
$11.9M
Small molecule protein-glycan inhib. as malaria transmission-blocking therapueticR01AI082587 · NIAID · JOHNS HOPKINS UNIVERSITY · PI DINGLASAN, RHOEL DAVID RAMOS · 2009 to 2013
$1.9M
Glycobiological Analysis of Plasmodium-Vector Host InteractionsK22AI077707 · NIAID · JOHNS HOPKINS UNIVERSITY · PI DINGLASAN, RHOEL DAVID RAMOS · 2009 to 2010
$270k
NHLBI NIH HHS HHSN268201000032CNHLBI NIH HHS N01-HV-00240NIAID NIH HHS 5T32AI007417-17NIAID NIH HHS K22 AI077707NIAID NIH HHS K22AI077707-02NIAID NIH HHS R01 AI082587NIAID NIH HHS R01AI082587-01NIAID NIH HHS T32 AI007417
6 · The paper itself

Abstract

Lipid raft microdomains, a component of detergent resistant membranes (DRMs), are routinely exploited by pathogens during host-cell entry. Multiple membrane-surface proteins mediate Plasmodium ookinete invasion of the Anopheles midgut, a critical step in the parasite life cycle that is successfully targeted by transmission-blocking vaccines (TBV). Given that lipid rafts are a common feature of host-pathogen interactions, we hypothesized that they promote the partitioning of midgut surface proteins and thus facilitate ookinete invasion. In support of this hypothesis, we found that five of the characterized Anopheles TBV candidates, including the leading Anopheles TBV candidate, AgAPN1, are present in Anopheles gambiae DRMs. Therefore, to extend the repertoire of putative midgut ligands that can be targeted by TBVs, we analyzed midgut DRMs by tandem mass spectrometry. We identified 1452 proteins including several markers of DRMs. Since glycosylphosphotidyl inositol (GPI)-anchored proteins partition to DRMs, we characterized the GPI subproteome of An. gambiae midgut brush-border microvilli and found that 96.9% of the proteins identified in the GPI-anchored fractions were also present in DRMs. Our study vastly expands the number of candidate malarial TBV targets for subsequent analysis by the broader community and provides an inferred role for midgut plasmalemma microdomains in ookinete cell invasion.

Indexed as

Host-Parasite InteractionsAnimalsAnophelesCholesterolDigestive SystemEpitheliumFemaleGlycosylationGPI-Linked ProteinsImmunoglobulinsInsect ProteinsMembrane MicrodomainsMicrovilliModels, BiologicalPlasmodiumProtein Structure, TertiaryCholesterolGPI-Linked ProteinsImmunoglobulinsInsect Proteins

Identifiers

PMID21905706
PMCPMC3208356

What OpenQuestion holds

Textmetadata
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.