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

J 2013

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

GARDNER, Christina L; Jo CHOI-NURVITADHI; Chengqun SUN; Avraham BAYER; Jozef HRITZ et al.

Základní údaje

Originální název

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

Autoři

GARDNER, Christina L; Jo CHOI-NURVITADHI; Chengqun SUN; Avraham BAYER; Jozef HRITZ; Kate D RYMAN a William B KLIMSTRA

Vydání

JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2013, 0022-538X

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 4.648

Označené pro přenos do RIV

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.1128/JVI.00937-13

UT WoS

000321590200029

Klíčová slova anglicky

ross-river-virus; sindbis virus; flavobacterium-heparinum

Štítky

ne MU

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 25. 2. 2014 13:09, Olga Křížová

Anotace

V originále

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.

Citovat

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. JOURNAL OF VIROLOGY. WASHINGTON: AMER SOC MICROBIOLOGY, 2013, roč. 87, č. 15, s. 8582-8590. ISSN 0022-538X. Dostupné z: https://doi.org/10.1128/JVI.00937-13.

@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 = {https://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://doi.org/10.1128/JVI.00937-13.

Přehled o publikaci