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United States Department of Agriculture

Agricultural Research Service

Title: Sequence Analysis of the Capsid Protein Gene of Vesicular Exanthema of Swine Virus A48 and Its Relationship to Other Calicivirus Capsid Proteins

item Neill, John
item Meyer, R - FADDL, USDA, APHIS, NVSL
item Seal, Bruce

Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: September 17, 1996
Publication Date: N/A

Technical Abstract: Vesicular exanthema of swine virus (VESV), the prototype calicivirus, is the etiologic agent of vesicular exanthema of swine (VES). VES is characterized by vesicle formation on the extremities, mouth and snout and causes abortions and stillbirths if infection occurs during pregnancy. VESV is considered an exotic agent in the United States. The single capsid dprotein gene of VESV serotype A48 was cloned and sequenced. The capsid protein open reading frame was encoded in the 3'-terminal 2427 bases of the genomic RNA. This region also contained a small, overlapping reading frame which encoded a basic protein of unknown function similar to that previously described for both animal and human caliciviruses. The VESV A48 capsid protein was 69% similar to the San Miguel sea lion virus serotype 1 (SMSV 1) and 89% similar to the SMSV serotype 4 capsid proteins. The six apparently functional regions previously identified in SMSV 1, SMSV 4, feline calicivirus and rabbit hemorrhagic disease virus capsid proteins (regions A through F) were present in VESV A48. Two sets of PCR primers were designed which directed amplification of the N-terminus of the capsid protein gene and the hypervariable region (region E) of the capsid protein of these and 7 additional SMSV serotypes. Alignment and phylogenetic analysis of the N-terminal sequences confirmed the close relationship of these viruses. Alignment analysis of the hypervariable region of the 10 viruses revealed that there is great variety of sequence in this region; however, highly conserved residues were identified which are also conserved in the E region of the FCV capsid protein gene. These conserved amino acid residues are probably necessary for a function conserved in the animal caliciviruses.

Last Modified: 4/22/2015
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