Neurovirulence for rats of the JHMV variants escaped from neutralization with the S1-specific monoclonal antibodies.
We have studied the neurovirulence for rats of the MAb-resistant variants isolated from a highly neurovirulent JHMV, cl-2. The variants, MM6 and MM13, with point mutation located within the N terminal 100 amino acids (aa) of the S1 protein showed no alteration in neurovirulence in comparison with cl-2, showing high neurovirulence. The variants, MM65 and MM85, with a deletion composed of about 150 aa located in the middle of the S1 subunit were revealed to be non-neurovirulent. A variant MM78 with one aa deletion, asparagic acid at number 543 from the N terminus of the S1, was shown to be low-virulence. The neurovirulence of these viruses paralleled with the viral growth potential in the rat brain. However, all of these variants as well as parental cl-2 showed high neurovirulence for mice. These results suggest that the domain composed of about 150 aa in the middle of the S1 is critical for high-neurovirulence of JHMV for rats.
Taguchi
F
F
National Institute of Neuroscience, NCNP, Tokyo, Japan.
Suzuki
H
H
Takahashi
H
H
Kubo
H
H
D000818:Animals; D000911:Antibodies, Monoclonal; D000918:Antibody Specificity; D018352:Coronavirus Infections / Q000276:immunology / Q000503:physiopathology*; D014644:Genetic Variation; D008562:Membrane Glycoproteins / Q000235:genetics* / Q000276:immunology; D051379:Mice; D006517:Murine hepatitis virus / Q000235:genetics / Q000276:immunology* / Q000472:pathogenicity*; D009500:Neutralization Tests; D017354:Point Mutation; D051381:Rats; D017384:Sequence Deletion; D013045:Species Specificity; D064370:Spike Glycoprotein, Coronavirus; D014759:Viral Envelope Proteins / Q000235:genetics* / Q000276:immunology; D014774:Virulence
D000911:Antibodies, Monoclonal; D008562:Membrane Glycoproteins; D064370:Spike Glycoprotein, Coronavirus; D014759:Viral Envelope Proteins