Title |
Amino acid differences in glycoproteins B (gB), C (gC), H (gH) and L(gL) are associated with enhanced herpes simplex virus type-1 (McKrae) entry via the paired immunoglobulin-like type-2 receptor α
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Published in |
Virology Journal, June 2012
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DOI | 10.1186/1743-422x-9-112 |
Pubmed ID | |
Authors |
Sona Chowdhury, Misagh Naderi, Vladimir N Chouljenko, Jason D Walker, Konstantin G Kousoulas |
Abstract |
Herpes simplex virus type-1 (HSV-1) enters into cells via membrane fusion of the viral envelope with plasma or endosomal membranes mediated by viral glycoproteins. HSV-1 virions attach to cell surfaces by binding of viral glycoproteins gC, gD and gB to specific cellular receptors. Here we show that the human ocular and highly neurovirulent HSV-1 strain McKrae enters substantially more efficiently into cells via the gB-specific human paired immunoglobulin-like type-2 receptor-α (hPILR-α). Comparison of the predicted amino acid sequences between HSV-1(F) and McKrae strains indicates that amino acid changes within gB, gC, gH and gL may cause increased entry via the hPILR- α receptor. |
X Demographics
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United States | 1 | 100% |
Demographic breakdown
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Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
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Unknown | 8 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Researcher | 4 | 50% |
Student > Ph. D. Student | 2 | 25% |
Student > Postgraduate | 1 | 13% |
Student > Doctoral Student | 1 | 13% |
Readers by discipline | Count | As % |
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Medicine and Dentistry | 3 | 38% |
Agricultural and Biological Sciences | 2 | 25% |
Veterinary Science and Veterinary Medicine | 1 | 13% |
Biochemistry, Genetics and Molecular Biology | 1 | 13% |
Unknown | 1 | 13% |