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Comparative Analysis of Glycoprotein B (gB) of Equine Herpesvirus Type 1 and Type 4 (EHV-1 and EHV-4) in Cellular Tropism and Cell-to-cell Transmission

Overview
Journal Viruses
Publisher MDPI
Specialty Microbiology
Date 2015 Feb 6
PMID 25654240
Citations 7
Authors
Affiliations
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Abstract

Glycoprotein B (gB) plays an important role in alphaherpesvirus cellular entry and acts in concert with gD and the gH/gL complex. To evaluate whether functional differences exist between gB1 and gB4, the corresponding genes were exchanged between the two viruses. The gB4-containing-EHV-1 (EHV-1_gB4) recombinant virus was analyzed for growth in culture, cell tropism, and cell entry rivaling no significant differences when compared to parental virus. We also disrupted a potential integrin-binding motif, which did not affect the function of gB in culture. In contrast, a significant reduction of plaque sizes and growth kinetics of gB1-containing-EHV-4 (EHV-4_gB1) was evident when compared to parental EHV-4 and revertant viruses. The reduction in virus growth may be attributable to the loss of functional interaction between gB and the other envelope proteins involved in virus entry, including gD and gH/gL. Alternatively, gB4 might have an additional function, required for EHV-4 replication, which is not fulfilled by gB1. In conclusion, our results show that the exchange of gB between EHV-1 and EHV-4 is possible, but results in a significant attenuation of virus growth in the case of EHV-4_gB1. The generation of stable recombinant viruses is a valuable tool to address viral entry in a comparative fashion and investigate this aspect of virus replication further.

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References
1.
Whalley J, Ruitenberg K, Sullivan K, Seshadri L, Hansen K, Birch D . Host cell tropism of equine herpesviruses: glycoprotein D of EHV-1 enables EHV-4 to infect a non-permissive cell line. Arch Virol. 2006; 152(4):717-25. DOI: 10.1007/s00705-006-0885-x. View

2.
Heldwein E, Lou H, Bender F, Cohen G, Eisenberg R, Harrison S . Crystal structure of glycoprotein B from herpes simplex virus 1. Science. 2006; 313(5784):217-20. DOI: 10.1126/science.1126548. View

3.
Farnsworth A, Wisner T, Webb M, Roller R, Cohen G, Eisenberg R . Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane. Proc Natl Acad Sci U S A. 2007; 104(24):10187-92. PMC: 1891206. DOI: 10.1073/pnas.0703790104. View

4.
Avitabile E, Forghieri C, Campadelli-Fiume G . Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein. J Virol. 2007; 81(20):11532-7. PMC: 2045520. DOI: 10.1128/JVI.01343-07. View

5.
Atanasiu D, Whitbeck J, Cairns T, Reilly B, Cohen G, Eisenberg R . Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion. Proc Natl Acad Sci U S A. 2007; 104(47):18718-23. PMC: 2141843. DOI: 10.1073/pnas.0707452104. View