Structure-Based Mutational Analysis of the Highly Conserved Domain IV of Glycoprotein H of Pseudorabies Virus
Journal of Virology, 07/16/2012
Fuchs W et al. – The gH function was also severely affected by disruption of the disulfide bond at the C terminus of the flap and after introduction of cysteine pairs designed to bridge the central part of the flap with the hydrophobic patch. Interestingly, all mutated gH proteins were able to complement gH–deleted PrV, but fusion–deficient gH mutants resulted in a pronounced delay in virus entry.