scholarly journals Serological responses in sheep injected with plasmids encoding bovine herpesvirus 1 (BHV-1) gD glycoprotein

2003 ◽  
Vol 55 (3) ◽  
pp. 256-261
Author(s):  
A.L. Cândido ◽  
M. Resende ◽  
L.R.G. Bessa ◽  
R.C. Leite

A genetic vaccine consisting of the bovine herpesvirus-1.2a (BHV-1.2a) glycoprotein D (gD) gene under the control of the cytomegalovirus immediate-early promoter/enhancer was generated and administered to sheep intramuscularly in the neck. All animals developed serum antibodies which recognized the homologous antigen (BHV-1.2a strain BH-83) and also exhibited cross-reactivity against the heterologous antigen (BHV-5 strain EVI-190). Three intramuscularly injections were given but serological responses were not improved after the second inoculation. Specific antibodies were detected against BHV-1.2a until at least 12 months after the first inoculation. However, the capacity to induce antibodies against BHV-5 was lower and of shorter duration than to BHV-1.2a.

2004 ◽  
Vol 35 (6) ◽  
pp. 715-721 ◽  
Author(s):  
Sacha Gogev ◽  
Jean-Pierre Georgin ◽  
Fr�d�ric Schynts ◽  
Alain Vanderplasschen ◽  
Etienne Thiry

Virus Genes ◽  
2014 ◽  
Vol 48 (3) ◽  
pp. 438-447 ◽  
Author(s):  
Carolina Kist Traesel ◽  
Mariana Sá e Silva ◽  
Marcelo Weiss ◽  
Fernando Rosado Spilki ◽  
Rudi Weiblen ◽  
...  

2020 ◽  
Vol 6 (20) ◽  
pp. eaba5147
Author(s):  
Dan Yue ◽  
Zhujun Chen ◽  
Fanli Yang ◽  
Fei Ye ◽  
Sheng Lin ◽  
...  

Bovine herpesvirus 1 (BHV-1) has received increasing attention for its potential oncolytic applications. BHV-1 recognizes nectin-1 for cell entry via viral glycoprotein D (gD) but represents a low-affinity nectin-1 binding virus. The molecular basis underlying this low receptor-binding affinity, however, remains unknown. Here, the crystal structures of BHV-1 gD in the free and nectin-1–bound forms are presented. While showing an overall resembled nectin-1 binding mode to other alphaherpesvirus gDs, BHV-1 gD has a unique G-strand/α2-helix interloop that disturbs gD/nectin-1 interactions. Residue R188 residing in this loop is observed to otherwise cause strong steric hindrance with the bound receptor, making a large conformational change of the loop a prerequisite for nectin-1 engagement. Subsequently, substitution of R188 with glycine markedly enhances the affinity of the BHV-1-gD/nectin-1 interaction (by about fivefold). These structural and functional data delineate the receptor-recognition basis for BHV-1, which might facilitate BHV-1–based oncolytic design in the future.


2006 ◽  
Vol 30 (S1) ◽  
pp. 257-259 ◽  
Author(s):  
S. Petrini ◽  
M. Ferrari ◽  
S. Vincenzetti ◽  
A. Vita ◽  
A. Amici ◽  
...  

Virology ◽  
1999 ◽  
Vol 261 (1) ◽  
pp. 143-152 ◽  
Author(s):  
Mohit K. Baxi ◽  
Lorne A. Babiuk ◽  
Majid Mehtali ◽  
Suresh K. Tikoo

Author(s):  
Barkha Ratta ◽  
Swagatika Priyadarsini ◽  
Nikhil K. Channabasappa ◽  
Pashupathi Mani ◽  
Meeta Saxena ◽  
...  

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