期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 282, 期 35, 页码 25376-25384出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M704698200
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资金
- NHLBI NIH HHS [R01 HL062244-05A1, R01 HL062244, HL52622, R01 HL052622, R01 HL062244-07, R01 HL052622-09, HL62244] Funding Source: Medline
- NIAID NIH HHS [R01 AI056840-02, AI056840, R01 AI056840] Funding Source: Medline
- NIGMS NIH HHS [R01 GM038060, R01 GM038060-19, GM38060] Funding Source: Medline
Heparan sulfate has been isolated for the first time from the mosquito Anopheles stephensi, a known vector for Plasmodium parasites, the causative agents of malaria. Chondroitin sulfate, but not dermatan sulfate or hyaluronan, was also present in the mosquito. The glycosaminoglycans were isolated, from salivary glands and midguts of the mosquito in quantities sufficient for disaccharide microanalysis. Both of these organs are invaded at different stages of the Plasmodium life cycle. Mosquito heparan sulfate was found to contain the critical trisulfated disaccharide sequence, -> 4)beta-D-GlcNS6S(1 -> 4)-alpha-L-IdoA2S(1 ->, that is commonly found in human liver heparan sulfate, which serves as the receptor for apolipoprotein E and is also believed to be responsible for binding to the circumsporozoite protein found on the surface of the Plasmodium sporozoite. The heparan sulfate isolated from the whole mosquito binds to circumsporozoite protein, suggesting a role within the mosquito for infection and transmission of the Plasmodium parasite.
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