4.4 Article

Characterization of Maguari orthobunyavirus mutants suggests the nonstructural protein NSm is not essential for growth in tissue culture

Journal

VIROLOGY
Volume 348, Issue 1, Pages 224-232

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2005.12.026

Keywords

bunyavirus; Maguari virus; nonstructural protein; glycoprotein

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Funding

  1. Wellcome Trust Funding Source: Medline

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Maguari virus (MAGV; genus Orthobunyavirus, family Bunyaviridae) contains a tripartite negative-sense RNA genome. Like all orthobunyaviruses, the medium (M) genome segment encodes a precursor polyprotein (NH2-Gn-NSm-Gc-COOH) for the two virion glycoproteins Gn and Cc and a nonstructural protein NSm. The nucleotide sequences of the M segment of wild-type (wt) MAGV, of a temperature-sensitive (ts) mutant, and of two non-ts revertants, R1 and R2, that show electrophoretic mobility differences in their Gc proteins were determined. Twelve amino acid differences (2 in Gn, 10 in Gc) were observed between wt and ts MAGV, of which 9 were maintained in R1 and R2. The M RNA segments of R1 and R2 contained internal deletions, resulting in the removal of the N-terminal 239 residues of Gc (R1) or the C-terminal two thirds of NSm and the N-terminal 431 amino acids of Gc (R2). The sequence data were consistent with analyses of the virion RNAs and virion glycoproteins. These results suggest that neither the N-terminal domain of Gc nor an intact NSm protein is required for the replication of MAGV in tissue culture. (c) 2005 Elsevier Inc. All rights reserved.

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