Abstract
The amino acid sequence of the gene for the peplomer protein of the vaccine strain M41 and the Beaudette laboratory strain M42-Salk of avian infectious bronchitis virus (IBV) have been derived from cDNA sequences. As found with other coronaviruses, the peplomer protein carries the epitopes eliciting neutralizing antibodies. The gene encodes a primary translation product of 1162 amino acids with a molecular weight of 128079. The use of a recent algorithm to predict membrane-protein interactions led to the unambiguous localization of the signah peptide and a transmembrane anchor α-helix at the C-terminus. At 50 positions amino acid differences were found between M41 and two Beaudette strains (M42-Salk and M42-Houghton). They are partly clustered in two regions of the protein. These two regions are candidates for neutralization epitopes of the protein.
Original language | English |
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Pages (from-to) | 253-263 |
Number of pages | 11 |
Journal | Virus Research |
Volume | 5 |
Issue number | 2-3 |
DOIs | |
Publication status | Published - 1 Jan 1986 |
Keywords
- coronavirus IBV
- M42
- peplomer protein
- strain M41