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@article{1166984, author = {Gardner, Christina L and ChoiandNurvitadhi, Jo and Sun, Chengqun and Bayer, Avraham and Hritz, Jozef and Ryman, Kate D and Klimstra, William B}, article_location = {WASHINGTON}, article_number = {15}, doi = {http://dx.doi.org/10.1128/JVI.00937-13}, keywords = {ross-river-virus; sindbis virus; flavobacterium-heparinum}, language = {eng}, issn = {0022-538X}, journal = {JOURNAL OF VIROLOGY}, title = {Natural Variation in the Heparan Sulfate Binding Domain of the Eastern Equine Encephalitis Virus E2 Glycoprotein Alters Interactions with Cell Surfaces and Virulence in Mice}, volume = {87}, year = {2013} }
TY - JOUR ID - 1166984 AU - Gardner, Christina L - Choi-Nurvitadhi, Jo - Sun, Chengqun - Bayer, Avraham - Hritz, Jozef - Ryman, Kate D - Klimstra, William B PY - 2013 TI - Natural Variation in the Heparan Sulfate Binding Domain of the Eastern Equine Encephalitis Virus E2 Glycoprotein Alters Interactions with Cell Surfaces and Virulence in Mice JF - JOURNAL OF VIROLOGY VL - 87 IS - 15 SP - 8582-8590 EP - 8582-8590 PB - AMER SOC MICROBIOLOGY SN - 0022538X KW - ross-river-virus KW - sindbis virus KW - flavobacterium-heparinum N2 - Recently, we compared amino acid sequences of the E2 glycoprotein of natural North American eastern equine encephalitis virus (NA-EEEV) isolates and demonstrated that naturally circulating viruses interact with heparan sulfate (HS) and that this interaction contributes to the extreme neurovirulence of EEEV (C. L. Gardner, G. D. Ebel, K. D. Ryman, and W. B. Klimstra, Proc. Natl. Acad. Sci. U. S. A., 108:16026-16031, 2011). In the current study, we have examined the contribution to HS binding of each of three lysine residues in the E2 71-to-77 region that comprise the primary HS binding site of wild-type (WT) NA-EEEV viruses. We also report that the original sequence comparison identified five virus isolates, each with one of three amino acid differences in the E2 71-to-77 region, including mutations in residues critical for HS binding by the WT virus. The natural variant viruses, which possessed either a mutation from lysine to glutamine at E2 71, a mutation from lysine to threonine at E2 71, or a mutation from threonine to lysine at E2 72, exhibited altered interactions with heparan sulfate and cell surfaces and altered virulence in a mouse model of EEEV disease. An electrostatic map of the EEEV E1/E2 heterotrimer based upon the recent Chikungunya virus crystal structure (J. E. Voss, M. C. Vaney, S. Duquerroy, C. Vonrhein, C. Girard-Blanc, E. Crublet, A. Thompson, G. Bricogne, and F. A. Rey, Nature, 468:709-712, 2010) showed the HS binding site to be at the apical surface of E2, with variants affecting the electrochemical nature of the binding site. Together, these results suggest that natural variation in the EEEV HS binding domain may arise during EEEV sylvatic cycles and that this variation may influence receptor interaction and the severity of EEEV disease. ER -
GARDNER, Christina L, Jo CHOI-NURVITADHI, Chengqun SUN, Avraham BAYER, Jozef HRITZ, Kate D RYMAN a William B KLIMSTRA. Natural Variation in the Heparan Sulfate Binding Domain of the Eastern Equine Encephalitis Virus E2 Glycoprotein Alters Interactions with Cell Surfaces and Virulence in Mice. \textit{JOURNAL OF VIROLOGY}. WASHINGTON: AMER SOC MICROBIOLOGY, 2013, roč.~87, č.~15, s.~8582-8590. ISSN~0022-538X. Dostupné z: https://dx.doi.org/10.1128/JVI.00937-13.
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