The fibrinogen-like domain of FREP1 protein is a broad-spectrum malaria transmission-blocking vaccine antigen

Guodong Niu; Caio M Franca; Genwei Zhang; Wanlapa Roobsoong; Wang Nguitragool; Xiaohong Wang; Jetsumon Prachumsri; Noah S Butler; Jun Li

doi:10.1074/jbc.m116.773564

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The fibrinogen-like domain of FREP1 protein is a broad-spectrum malaria transmission-blocking vaccine antigen

Journal article

Open access

Peer reviewed

The fibrinogen-like domain of FREP1 protein is a broad-spectrum malaria transmission-blocking vaccine antigen

Guodong Niu, Caio M Franca, Genwei Zhang, Wanlapa Roobsoong, Wang Nguitragool, Xiaohong Wang, Jetsumon Prachumsri, Noah S Butler and Jun Li

The Journal of biological chemistry, Vol.292(28), pp.11960-11969

07/14/2017

DOI: 10.1074/jbc.m116.773564

PMCID: PMC5512087

PMID: 28533429

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Abstract

FREP1 in mosquito midguts facilitates parasite transmission. The fibrinogen-like (FBG) domain of FREP1 is highly conserved (>90% identical) among species from different continents, suggesting that anti-FBG antibodies may block malaria transmission to all anopheline mosquitoes. Using standard membrane-feeding assays, anti-FREP1 polyclonal antibodies significantly blocked transmission of and to and , respectively. Furthermore, studies of mice immunized with FBG achieved >75% blocking efficacy of to without triggering immunopathology. Anti-FBG serum also reduced >81% of infection to Finally, we showed that FBG interacts with gametocytes and ookinetes, revealing the molecular mechanism of its antibody transmission-blocking activity. Collectively, our data support that FREP1-mediated transmission to mosquitoes is a conserved pathway and that targeting the FBG domain of FREP1 will limit the transmission of multiple species to multiple species.

Anopheles - metabolism

Plasmodium vivax - growth & development

Recombinant Proteins - therapeutic use

Plasmodium berghei - immunology

Malaria, Falciparum - prevention & control

Species Specificity

Humans

Antibodies, Blocking - analysis

Male

Plasmodium falciparum - immunology

Malaria Vaccines - chemistry

Malaria, Falciparum - transmission

Malaria, Vivax - blood

Vaccines, Synthetic - metabolism

Conserved Sequence

Female

Insect Proteins - therapeutic use

Malaria Vaccines - therapeutic use

Protein Interaction Domains and Motifs

Germ Cells - metabolism

Insect Proteins - metabolism

Peptide Fragments - genetics

Vaccines, Synthetic - chemistry

Recombinant Proteins - metabolism

Amino Acid Sequence

Peptide Fragments - metabolism

Anopheles - parasitology

Malaria, Vivax - parasitology

Insect Proteins - genetics

Recombinant Proteins - chemistry

Vaccines, Synthetic - therapeutic use

Plasmodium vivax - immunology

Sequence Homology, Amino Acid

Malaria, Falciparum - parasitology

Peptide Fragments - chemistry

Sequence Alignment

Animals

Insect Proteins - chemistry

Malaria, Falciparum - immunology

Plasmodium berghei - growth & development

Malaria, Vivax - immunology

Mice

Peptide Fragments - therapeutic use

Plasmodium falciparum - growth & development

Anopheles - immunology

Malaria Vaccines - metabolism

Germ Cells - immunology

Malaria Vaccines - genetics

Details

Title: Subtitle: The fibrinogen-like domain of FREP1 protein is a broad-spectrum malaria transmission-blocking vaccine antigen
Creators: Guodong Niu - the Department of Biological Sciences, Florida International University, Miami, Florida 33199
Caio M Franca - From the Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019
Genwei Zhang - From the Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019
Wanlapa Roobsoong - the Mahidol Vivax Research Center, Mahidol University Faculty of Tropical Medicine, Bangkok 10400, Thailand
Wang Nguitragool - the Mahidol Vivax Research Center, Mahidol University Faculty of Tropical Medicine, Bangkok 10400, Thailand
Xiaohong Wang - the Department of Biological Sciences, Florida International University, Miami, Florida 33199
Jetsumon Prachumsri - the Mahidol Vivax Research Center, Mahidol University Faculty of Tropical Medicine, Bangkok 10400, Thailand
Noah S Butler - the Department of Microbiology and Immunology, University of Iowa, Iowa City, Iowa 52242, and
Jun Li - From the Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.292(28), pp.11960-11969
DOI: 10.1074/jbc.m116.773564
PMID: 28533429
PMCID: PMC5512087
NLM abbreviation: J Biol Chem
ISSN: 1083-351X
eISSN: 1083-351X
Publisher: United States
Grant note: R21 AI115178 / NIAID NIH HHS R01 AI125657 / NIAID NIH HHS
Language: English
Date published: 07/14/2017
Academic Unit: Microbiology and Immunology
Record Identifier: 9984001131302771

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