Evidence map›Paper›PMID 28819256›Full record

ArticleScientific reports2017

FBN30 in wild Anopheles gambiae functions as a pathogen recognition molecule against clinically circulating Plasmodium falciparum in malaria endemic areas in Kenya.

Guodong Niu, Genwei Zhang, Caio Franca, Yingjun Cui, Stephen Munga, Yaw Afrane, Jun Li

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 27% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. 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

7 authors at 3 institutions in 2 countries.

Guodong NiuDepartment of Biological Sciences, Biomolecular Sciences Institute, Florida International University, Miami, Florida, 33199, USA.
Genwei ZhangDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma, 73019, USA.
Caio FrancaDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma, 73019, USA.ORCID 0000-0002-5056-7983
Yingjun CuiDepartment of Biological Sciences, Biomolecular Sciences Institute, Florida International University, Miami, Florida, 33199, USA.
Stephen MungaCentre for Global Health Research, Kenya Medical Research Institute, Kisumu, Kenya.
Yaw AfraneCentre for Global Health Research, Kenya Medical Research Institute, Kisumu, Kenya.
Jun LiDepartment of Biological Sciences, Biomolecular Sciences Institute, Florida International University, Miami, Florida, 33199, USA. lij@fiu.edu.
Florida International University · USKenya Medical Research Institute · KEUniversity of Oklahoma · US

Funding

Fungal metabolites block malaria transmissionR01AI125657 · NIAID · FLORIDA INTERNATIONAL UNIVERSITY · PI LI, JUN · 2017 to 2021
$2.5M
Targeting Mosquito FREP1 Protein for Malaria ControlR21AI115178 · NIAID · UNIVERSITY OF OKLAHOMA · PI LI, JUN · 2015 to 2016
$421k
NIAID NIH HHS R01 AI125657NIAID NIH HHS R21 AI115178
6 · The paper itself

Abstract

Malaria is a worldwide health problem that affects two-thirds of the world population. Plasmodium invasion of anopheline mosquitoes is an obligatory step for malaria transmission. However, mosquito-malaria molecular interactions in nature are not clear. A genetic variation within mosquito fibrinogen related-protein 30 (FBN30) was previously identified to be associated with Plasmodium falciparum infection in natural Anopheles gambiae populations at malaria endemic areas in Kenya, and reducing FBN30 expression by RNAi makes mosquitoes more susceptible to P. berghei. New results show that FBN30 is a secreted octamer that binds to both P. berghei and clinically circulating P. falciparum from malaria endemic areas in Kenya, but not laboratory P. falciparum strain NF54. Moreover, the natural genetic mutation (T to C) within FBN30 signal peptide, which changes the position 10 amino acid from phenylalanine to leucine, reduces protein expression by approximately half. This change is consistent to more susceptible An. gambiae to P. falciparum infection in the field. FBN30 in natural An. gambiae is proposed to work as a pathogen recognition molecule in inhibiting P. falciparum transmission in malaria endemic areas.

Indexed as

AnimalsAnophelesCell LineEndemic DiseasesHost-Parasite InteractionsHumansInsect ProteinsKenyaMalariaMutationPlasmodium bergheiPlasmodium falciparumProtein BindingProtein MultimerizationProtein Sorting SignalsInsect ProteinsProtein Sorting Signals

Identifiers

PMID28819256
PMCPMC5561218
OpenAlexW2744552280

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.