期刊
BIOCHEMICAL JOURNAL
卷 438, 期 -, 页码 475-483出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20110694
关键词
Anopheles; cell invasion; glycobiology; glycosaminoglycan (GAG); heparan sulfate (HS); malaria
资金
- Austrian Fonds zur Forderung der wissenschaftlichen Forschung [L314]
- National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH) [1K22AI077707]
- Malaria Research Institute, Johns Hopkins Bloomberg School of Public Health (JHMRI)
- NIH National Center for Research Resources [UL1 RR 0250051]
- Austrian Science Fund (FWF) [L314] Funding Source: Austrian Science Fund (FWF)
HS (heparan sulfate) has been shown to be an important mediator of Plasmodium sporozoite homing and invasion of the liver, but the role of this glycosaminoglycan in mosquito vector host-sporozoite interactions is unknown. We have biochemically characterized the function of AgOXT1 (Anopheles gambiae peptide-O-xylosyltransferase 1) and confirmed that AgOXT 1 can modify peptides representing model HS and chondroitin sulfate proteoglycans in vitro. Moreover, we also demonstrated that the mosquito salivary gland basal lamina proteoglycans are modified by HS. We used RNA interference-mediated knockdown of HS biosynthesis in A. gambiae salivary glands to determine whether Plasmodium falciparum sporozoites that are released from mosquito midgut oocysts use salivary gland HS as a receptor for tissue invasion. Our results suggest that salivary gland basal lamina HS glycosaminoglycans only partially mediate midgut sporozoite invasion of this tissue, and that in the absence of HS, the presence of other surface co-receptors is sufficient to facilitate parasite entry.
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