The selection pressure analysis of classical swine fever virus envelope protein genes Erns and E2

2008 ◽  
Vol 131 (2) ◽  
pp. 132-135 ◽  
Author(s):  
Fangqiang Tang ◽  
Zishu Pan ◽  
Chuyu Zhang
Keyword(s):  
Classical Swine Fever Virus ◽  
Envelope Protein ◽  
Selection Pressure ◽  
Classical Swine Fever ◽  
Fever Virus ◽  
Virus Envelope ◽  
Virus Envelope Protein ◽  
Pressure Analysis

scholarly journals Characterization and molecular basis of heterogeneity of the African swine fever virus envelope protein p54.

1994 ◽  
Vol 68 (11) ◽  
pp. 7244-7252 ◽  
Author(s):  
F Rodriguez ◽  
C Alcaraz ◽  
A Eiras ◽  
R J Yáñez ◽  
J M Rodriguez ◽  
...  
Keyword(s):  
Envelope Protein ◽  
Molecular Basis ◽  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Fever Virus ◽  
Virus Envelope ◽  
Virus Envelope Protein

scholarly journals Different evolutionary patterns of classical swine fever virus envelope proteins

2016 ◽  
Vol 62 (3) ◽  
pp. 210-219 ◽  
Author(s):  
Yan Li ◽  
Zexiao Yang ◽  
Mingwang Zhang
Keyword(s):  
Classical Swine Fever Virus ◽  
Functional Divergence ◽  
Classical Swine Fever ◽  
Acid Sites ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
Fever Virus ◽  
Host Cells ◽  
Virus Envelope ◽  
Evolutionary Patterns

Classical swine fever virus (CSFV) is the causative agent of classical swine fever, which is a highly contagious disease of the domestic pig as well as wild boar. The proteins Erns, E1, and E2 are components of the viral envelope membrane. They are also implicated in virus attachment and entry, replication, and (or) anti-immune response. Here, we studied the genetic variations of these envelope proteins in the evolution of CSFV. The results reveal that the envelope proteins underwent different evolutionary fates. In Ernsand E1, but not E2, a number of amino acid sites experienced functional divergence. Furthermore, the diversification in Ernsand E1 was generally episodic because the divergence-related changes of E1 only occurred with the separation of 2 major groups of CSFV and that of Ernstook place with the division of 1 major group. The major divergence-related sites of Ernsare located on one of the substrate-binding regions of the RNase domain and C-terminal extension. These functional domains have been reported to block activation of the innate immune system and attachment and entry into host cells, respectively. Our results may shed some light on the divergent roles of the envelope proteins.

NMR assignments of the yellow fever virus envelope protein domain III

2007 ◽  
Vol 1 (1) ◽  
pp. 49-50 ◽  
Author(s):  
David E. Volk ◽  
Sai H. A. Gandham ◽  
Fiona J. May ◽  
Anjenique Anderson ◽  
Alan D. T. Barrett ◽  
...  
Keyword(s):  
Yellow Fever ◽  
Envelope Protein ◽  
Nmr Assignments ◽  
Yellow Fever Virus ◽  
Fever Virus ◽  
Protein Domain ◽  
Virus Envelope ◽  
Virus Envelope Protein ◽  
Domain Iii

Positive selection pressure on the B/C domains of the E2-gene of classical swine fever virus in endemic areas under C-strain vaccination

2012 ◽  
Vol 12 (7) ◽  
pp. 1405-1412 ◽  
Author(s):  
Lester Josué Pérez ◽  
Heidy Díaz de Arce ◽  
Carmen Laura Perera ◽  
Rosa Rosell ◽  
Maria T. Frías ◽  
...  
Keyword(s):  
Positive Selection ◽  
Classical Swine Fever Virus ◽  
Selection Pressure ◽  
Classical Swine Fever ◽  
Fever Virus ◽  
Positive Selection Pressure ◽  
E2 Gene ◽  
Endemic Areas

scholarly journals Yellow fever virus envelope protein has two discrete type-specific neutralizing epitopes.

1997 ◽  
Vol 78 (6) ◽  
pp. 1353-1356 ◽  
Author(s):  
K D Ryman ◽  
A D Barrett ◽  
J J Schlesinger ◽  
R C Weir ◽  
T N Ledger
Keyword(s):  
Yellow Fever ◽  
Envelope Protein ◽  
Yellow Fever Virus ◽  
Fever Virus ◽  
Virus Envelope ◽  
Virus Envelope Protein ◽  
Neutralizing Epitopes ◽  
Discrete Type
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