Identification of plasmodium GAPDH epitopes for generation of antibodies that inhibit malaria infection

Sung-Jae Cha, Kyle Jarrod McLean, Marcelo Jacobs-Lorena

Research output: Contribution to journalArticle

Abstract

Plasmodium sporozoite liver infection is an essential step for parasite development in its mammalian host. Previously, we used a phage display library to identify mimotope peptides that bind to Kupffer cells and competitively inhibit sporozoite–Kupffer cell interaction. These peptides led to the identification of a Kupffer cell receptor—CD68—and a Plasmodium sporozoite ligand—GAPDH—that are required for sporozoite traversal of Kupffer cells and subsequent infection of hepatocytes. Here, we report that the C-terminal end of Plasmodium GAPDH interacts with the Kupffer CD68 receptor, and identify two epitopes within this region as candidate antigens for the development of antibodies that inhibit Plasmodium infection.

Original languageEnglish (US)
Article numbere201800111
JournalLife Science Alliance
Volume1
Issue number5
DOIs
StatePublished - Jan 1 2018

Fingerprint

Sporozoites
Kupffer Cells
Plasmodium
malaria
Kupffer cells
epitopes
Malaria
antibody
sporozoites
Epitopes
peptide
antibodies
Antibodies
Infection
infection
Peptides
Bacteriophages
peptides
antigen
Cell Communication

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology (miscellaneous)
  • Plant Science
  • Ecology
  • Health, Toxicology and Mutagenesis

Cite this

Identification of plasmodium GAPDH epitopes for generation of antibodies that inhibit malaria infection. / Cha, Sung-Jae; McLean, Kyle Jarrod; Jacobs-Lorena, Marcelo.

In: Life Science Alliance, Vol. 1, No. 5, e201800111, 01.01.2018.

Research output: Contribution to journalArticle

@article{b2cd2de90d184878b690d4269bd3f625,
title = "Identification of plasmodium GAPDH epitopes for generation of antibodies that inhibit malaria infection",
abstract = "Plasmodium sporozoite liver infection is an essential step for parasite development in its mammalian host. Previously, we used a phage display library to identify mimotope peptides that bind to Kupffer cells and competitively inhibit sporozoite–Kupffer cell interaction. These peptides led to the identification of a Kupffer cell receptor—CD68—and a Plasmodium sporozoite ligand—GAPDH—that are required for sporozoite traversal of Kupffer cells and subsequent infection of hepatocytes. Here, we report that the C-terminal end of Plasmodium GAPDH interacts with the Kupffer CD68 receptor, and identify two epitopes within this region as candidate antigens for the development of antibodies that inhibit Plasmodium infection.",
author = "Sung-Jae Cha and McLean, {Kyle Jarrod} and Marcelo Jacobs-Lorena",
year = "2018",
month = "1",
day = "1",
doi = "10.26508/lsa.201800111",
language = "English (US)",
volume = "1",
journal = "Life Science Alliance",
issn = "2575-1077",
publisher = "Rockefeller University Press",
number = "5",

}

TY - JOUR

T1 - Identification of plasmodium GAPDH epitopes for generation of antibodies that inhibit malaria infection

AU - Cha, Sung-Jae

AU - McLean, Kyle Jarrod

AU - Jacobs-Lorena, Marcelo

PY - 2018/1/1

Y1 - 2018/1/1

N2 - Plasmodium sporozoite liver infection is an essential step for parasite development in its mammalian host. Previously, we used a phage display library to identify mimotope peptides that bind to Kupffer cells and competitively inhibit sporozoite–Kupffer cell interaction. These peptides led to the identification of a Kupffer cell receptor—CD68—and a Plasmodium sporozoite ligand—GAPDH—that are required for sporozoite traversal of Kupffer cells and subsequent infection of hepatocytes. Here, we report that the C-terminal end of Plasmodium GAPDH interacts with the Kupffer CD68 receptor, and identify two epitopes within this region as candidate antigens for the development of antibodies that inhibit Plasmodium infection.

AB - Plasmodium sporozoite liver infection is an essential step for parasite development in its mammalian host. Previously, we used a phage display library to identify mimotope peptides that bind to Kupffer cells and competitively inhibit sporozoite–Kupffer cell interaction. These peptides led to the identification of a Kupffer cell receptor—CD68—and a Plasmodium sporozoite ligand—GAPDH—that are required for sporozoite traversal of Kupffer cells and subsequent infection of hepatocytes. Here, we report that the C-terminal end of Plasmodium GAPDH interacts with the Kupffer CD68 receptor, and identify two epitopes within this region as candidate antigens for the development of antibodies that inhibit Plasmodium infection.

UR - http://www.scopus.com/inward/record.url?scp=85057054185&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85057054185&partnerID=8YFLogxK

U2 - 10.26508/lsa.201800111

DO - 10.26508/lsa.201800111

M3 - Article

VL - 1

JO - Life Science Alliance

JF - Life Science Alliance

SN - 2575-1077

IS - 5

M1 - e201800111

ER -