Comparison of the sequence of the secretory glycoprotein A (gA) gene in Md5 and BC-1 strains of Marek's disease virus type 1

✍ Scribed by Takeshi Ihara; Atsushi Kato; Susumu Ueda; Akira Ishihama; Kanji Hirai

• Publisher: Springer
• Year: 1989
• Tongue: English
• Weight: 783 KB
• Volume: 3
• Category: Article
• ISSN: 0920-8569
• DOI: 10.1007/bf00125125

✦ Synopsis

DNA fragments containing the secretory glycoprotein A (gA) gene of Marek's disease virus type 1 (MDVI) were cloned from the DNA libraries of very virulent Md5 and virulent BC-I strains and sequenced. Two open reading frames (ORFl and ORF2) were identified for both strains. The ORFI has the potential to code for a protein of 501 amino acids with a molecular weight of 56 kD that contains strong hydrophobic regions in both the amino and carboxyl termini, and nine potential Nlinked glycosylation sites, while the ORF2 is capable of coding for a 24-kD protein. These results indicate that the ORFI codes for the unprocessed form of gA. Between the Md5 and BC-I strains, only two sequence mismatches exist in the DNA fragment. More differences appear to exist in the gA sequence of the MDV I GA strain (12), which lacks a strong hydrophobic anchor sequence. Similarities between the predicted amino acid sequences of the MDV I gA and the proteins of the other herpesviruses such as hewes simplex type I gC, pseudorabies virus gII1, and varicella zoster virus gpV were noted.