Heat Shock Protein 90 and Heat Shock Protein 70 Are Components of Dengue Virus Receptor Complex in Human Cells Export

@article{citeulike:4947508, abstract = {Dengue virus requires the presence of an unidentified cellular receptor on the surface of the host cell. By using a recently published affinity chromatography approach, an 84-kDa molecule, identified as heat shock protein 90 (HSP90) by matrix-assisted laser desorption ionization-time of flight mass spectrometry, was isolated from neuroblastoma and U937 cells. Based on the ability of HSP90 (84 kDa) to interact with HSP70 (74 kDa) on the surface of monocytes during lipopolysaccharide (LPS) signaling and evidence that LPS inhibits dengue virus infection, the presence of HSP70 was demonstrated in affinity chromatography eluates and by pull-down experiments. Infection inhibition assays support the conclusion that HSP90 and HSP70 participate in dengue virus entry as a receptor complex in human cell lines as well as in monocytes/macrophages. Additionally, our results indicate that both HSPs are associated with membrane microdomains (lipid rafts) in response to dengue virus infection. Moreover, methyl-{beta}-cyclodextrin, a raft-disrupting drug, inhibits dengue virus infection, supporting the idea that cholesterol-rich membrane fractions are important in dengue virus entry. 10.1128/JVI.79.8.4557-4567.2005}, author = {Reyes-Del and Chavez-Salinas, Salvador and Medina, Fernando and Del}, citeulike-article-id = {4947508}, citeulike-linkout-0 = {http://dx.doi.org/10.1128/JVI.79.8.4557-4567.2005}, citeulike-linkout-1 = {http://jvi.asm.org/cgi/content/abstract/79/8/4557}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/15795242}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=15795242}, doi = {10.1128/JVI.79.8.4557-4567.2005}, journal = {J. Virol.}, keywords = {dengue, hsp}, month = {April}, number = {8}, pages = {4557--4567}, posted-at = {2009-06-24 21:03:31}, priority = {2}, title = {Heat Shock Protein 90 and Heat Shock Protein 70 Are Components of Dengue Virus Receptor Complex in Human Cells}, url = {http://dx.doi.org/10.1128/JVI.79.8.4557-4567.2005}, volume = {79}, year = {2005} }

TY - JOUR ID - citeulike:4947508 L3 - citeulike-article-id:4947508 N2 - Dengue virus requires the presence of an unidentified cellular receptor on the surface of the host cell. By using a recently published affinity chromatography approach, an 84-kDa molecule, identified as heat shock protein 90 (HSP90) by matrix-assisted laser desorption ionization-time of flight mass spectrometry, was isolated from neuroblastoma and U937 cells. Based on the ability of HSP90 (84 kDa) to interact with HSP70 (74 kDa) on the surface of monocytes during lipopolysaccharide (LPS) signaling and evidence that LPS inhibits dengue virus infection, the presence of HSP70 was demonstrated in affinity chromatography eluates and by pull-down experiments. Infection inhibition assays support the conclusion that HSP90 and HSP70 participate in dengue virus entry as a receptor complex in human cell lines as well as in monocytes/macrophages. Additionally, our results indicate that both HSPs are associated with membrane microdomains (lipid rafts) in response to dengue virus infection. Moreover, methyl-{beta}-cyclodextrin, a raft-disrupting drug, inhibits dengue virus infection, supporting the idea that cholesterol-rich membrane fractions are important in dengue virus entry. 10.1128/JVI.79.8.4557-4567.2005 IS - 8 JF - J. Virol. EP - 4567 TI - Heat Shock Protein 90 and Heat Shock Protein 70 Are Components of Dengue Virus Receptor Complex in Human Cells VL - 79 SP - 4557 KW - dengue KW - hsp AU - Reyes-Del AU - Chavez-Salinas, Salvador AU - Medina, Fernando AU - Del PY - 2005/04/15/ UR - http://dx.doi.org/10.1128/JVI.79.8.4557-4567.2005 ER -