Abstract
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)β-D-GlcNS6S(1 → 4)-α-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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 25376-25384 |
| Number of pages | 9 |
| Journal | Journal of Biological Chemistry |
| Volume | 282 |
| Issue number | 35 |
| DOIs | |
| State | Published - Aug 31 2007 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Mosquito heparan sulfate and its potential role in malaria infection and transmission. / Sinnis, Photini; Coppi, Alida; Toida, Toshihiko; Toyoda, Hidenao; Kinoshita-Toyoda, Akiko; Xie, Jin; Kemp, Melissa M.; Linhardt, Robert J.
In: Journal of Biological Chemistry, Vol. 282, No. 35, 31.08.2007, p. 25376-25384.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Mosquito heparan sulfate and its potential role in malaria infection and transmission
AU - Sinnis, Photini
AU - Coppi, Alida
AU - Toida, Toshihiko
AU - Toyoda, Hidenao
AU - Kinoshita-Toyoda, Akiko
AU - Xie, Jin
AU - Kemp, Melissa M.
AU - Linhardt, Robert J.
PY - 2007/8/31
Y1 - 2007/8/31
N2 - 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)β-D-GlcNS6S(1 → 4)-α-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.
AB - 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)β-D-GlcNS6S(1 → 4)-α-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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UR - http://www.scopus.com/inward/citedby.url?scp=34548480687&partnerID=8YFLogxK
U2 - 10.1074/jbc.M704698200
DO - 10.1074/jbc.M704698200
M3 - Article
VL - 282
SP - 25376
EP - 25384
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 35
ER -