The highly conserved proline at position 438 in pseudorabies virus gH is important for regulation of membrane fusion.

ABSTRACT:

Unlabelled

Membrane fusion in herpesviruses requires viral glycoproteins (g) gB and gH/gL. While gB is considered the actual fusion protein but is nonfusogenic per se, the function of gH/gL remains enigmatic. Crystal structures for different gH homologs are strikingly similar despite only moderate amino acid sequence conservation. A highly conserved sequence motif comprises the residues serine-proline-cysteine corresponding to positions 437 to 439 in pseudorabies virus (PrV) gH. The PrV-gH structure shows that proline(438) induces bending at the end of an alpha-helix, thereby placing cysteine(404) and cysteine(439) in juxtaposition to allow formation of a strictly conserved disulfide bond. However, PrV vaccine strain Bartha unexpectedly carries a serine at this conserved position.

SUBMITTER: Schroter C 

PROVIDER: S-EPMC4249067 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature