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Journal of Virology, September 2007, p. 9611, Vol. 81, No. 18
0022-538X/07/$08.00+0     doi:10.1128/JVI.01609-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

SPOTLIGHT

Articles of Significant Interest Selected from This Issue by the Editors

The Cellular Protein eEF1A Facilitates West Nile Virus Minus-Strand RNA Synthesis

There are one major and two minor binding sites for eEF1A on the West Nile virus (WNV) genomic 3'-terminal stem-loop RNA. Davis et al. (p. 10172-10187) introduced mutations into the major binding site in a WNV infectious clone. Mutations that decreased eEF1A binding activity for the viral RNA in vitro decreased viral minus-strand RNA synthesis, whereas mutations that increased binding increased minus-strand synthesis. eEF1A coprecipitated and colocalized with flavivirus replication complex proteins and bound to the 3' RNAs of divergent flaviviruses. These results support the functional relevance of the viral RNA-eEF1A interaction for flavivirus minus-strand RNA synthesis.

Severe Acute Respiratory Syndrome Coronavirus ORF6 Antagonizes STAT1 Function

Severe acute respiratory syndrome coronavirus (SARS-CoV) is a virulent pathogen of humans that does not induce type I interferons (IFNs). Frieman et al. (p. 9812-9824) show that the virally encoded ORF6 protein blocks the nuclear import of the IFN transactivator, STAT1. ORF6 is localized on the endoplasmic reticulum (ER)/Golgi membrane where it specifically binds the nuclear import factor, karyopherin {alpha}2. The ORF6-karyopherin {alpha}2 complex tethers karyopherin ß1 onto the ER/Golgi membrane and limits its availability for association with the nuclear import machinery. Thus, diminished amounts of karyopherin ß1 prevent STAT1-karyopherin {alpha}1 import into the nucleus in response to IFN treatment.

Structural Insight into Minute Virus of Mice Neutralization by Antibody

Knowledge about neutralizing mechanisms of antibodies and how viruses escape their neutralizing power are the basis for vaccine development. Kaufmann et al. (p. 9851-9858) show how a neutralizing Fab molecule recognizes an epitope close to the threefold vertex on the surface of minute virus of mice, thereby simultaneously engaging three symmetry-related viral proteins. Thus, the Fab fragment might hinder structural transitions essential for viral entry. The mode of binding also facilitates viral escape from antibody recognition, as a single mutation could entail the simultaneous replacement of two or three residues forming the epitope, leading to a substantial reduction of antigen-antibody interactions.

CD40 Regulates T Cell Trafficking into the Brain after West Nile Virus Infection

Binding of CD40 by CD40 ligand (CD40L) on activated CD4+ T cells provides a costimulatory signal for antibody maturation and T-cell priming. Sitati et al. (p. 9801-9811) show that CD8+ T-cell trafficking to the brain after West Nile virus (WNV) infection is markedly impaired in CD40–/– mice, which results in uncontrolled viral infection and death. Immunohistochemistry of brains from infected CD40–/– mice revealed that T cells were retained in the perivascular space and did not migrate into the parenchyma, the site of WNV infection. These results suggest a novel function of CD40-CD40L interactions to facilitate T-cell migration across the blood-brain barrier to control viral infection.

Intragenic Recombination in Rotaviruses

G1 rotavirus is the most widespread genotype causing acute gastroenteritis in children. Phan et al. (p. 10188-10194) provide evidence for two different types of intragenic recombination (interlineage and intersublineage) in rotavirus VP7 genes. Although crucial contributions of genetic reassortment and nucleotide substitution are recognized in producing antigenic variants of rotavirus, these results indicate an important role for intragenic recombination in rotavirus evolution.

Journal of Virology, September 2007, p. 9611, Vol. 81, No. 18
0022-538X/07/$08.00+0     doi:10.1128/JVI.01609-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.




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