Site-directed mutagenesis of Autographa californica nucleopolyhedrovirus (AcNPV) polyhedrin: effect on polyhedron structure.

Abstract:

:Amino acids Lys34, His36, and Phe37 were substituted by PCR-mediated, site-directed mutagenesis for three Trp's in the AcNPV polyhedrin sequence. Phase contrast microscopy revealed refringent, amorphous polyhedra in the nuclei of infected cells. Electron microscopy confirmed a great variation in form and size of the mutated polyhedra. Although crystallization of the mutated polyhedrin occurred, it was irregular within each polyhedron. Virion occlusion was also severely affected. Virions were partially occluded, or only one virion was occluded per polyhedron. Results suggest that the substitution of these three amino acids affected the morphology of polyhedra, the uniformity of crystallization within each polyhedron, and the virion occlusion.

journal_name

Arch Virol

journal_title

Archives of virology

authors

Bravo-Patiño A,Ibarra JE

doi

10.1007/s007050050675

keywords:

subject

Has Abstract

pub_date

2000-01-01 00:00:00

pages

827-34

issue

4

eissn

0304-8608

issn

1432-8798

journal_volume

145

pub_type

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