scholarly journals Small plaque size variant of chikungunya primary isolate showed reduced virulence in mice

1972 ◽  
Vol 70 (1) ◽  
pp. 49-53 ◽  
Author(s):  
Janine J. Gould ◽  
Gwenneth D. Laurence ◽  
M. Butler

SUMMARYIn a comparative study of 24 different rubella virus strains, all but three formed small plaques in RK 13 cell cultures; of these one was the vaccine strain HPV-77, one was isolated from a congenitally infected infant, and the third was recovered from an adult who contracted severe rubella while handling this congenital strain. Whereas the plaque size of the vaccine strain was stable after further passage in cell culture, the plaque size of the other two rapidly diminished when the virus was passed in monkey kidney cells, and one of them was also reduced by passage in RK 13 cells. Cell culture passage of the typical small plaque strains did not result in altered plaque size.


Viruses ◽  
2021 ◽  
Vol 14 (1) ◽  
pp. 55
Author(s):  
Gi Uk Jeong ◽  
Gun Young Yoon ◽  
Hyun Woo Moon ◽  
Wooseong Lee ◽  
Insu Hwang ◽  
...  

SARS-CoV-2, like other RNA viruses, has a propensity for genetic evolution owing to the low fidelity of its viral polymerase. Several recent reports have described a series of novel SARS-CoV-2 variants. Some of these have been identified as variants of concern (VOCs), including alpha (B.1.1.7, Clade GRY), beta (B.1.351, Clade GH), gamma (P.1, Clade GR), and delta (B.1.617.2, Clade G). VOCs are likely to have some effect on transmissibility, antibody evasion, and changes in therapeutic or vaccine effectiveness. However, the physiological and virological understanding of these variants remains poor. We demonstrated that these four VOCs exhibited differences in plaque size, thermal stability at physiological temperature, and replication rates. The mean plaque size of beta was the largest, followed by those of gamma, delta, and alpha. Thermal stability, evaluated by measuring infectivity and half-life after prolonged incubation at physiological temperature, was correlated with plaque size in all variants except alpha. However, despite its relatively high thermal stability, alpha’s small plaque size resulted in lower replication rates and fewer progeny viruses. Our findings may inform further virological studies of SARS-CoV-2 variant characteristics, VOCs, and variants of interest. These studies are important for the effective management of the COVID-19 pandemic.


2005 ◽  
Vol 86 (5) ◽  
pp. 1403-1413 ◽  
Author(s):  
Thomas J. Chambers ◽  
Deborah A. Droll ◽  
Yujia Tang ◽  
Yan Liang ◽  
Vannakambadi K. Ganesh ◽  
...  

A series of 46 charged-to-alanine mutations in the yellow fever virus NS2B–NS3 protease, previously characterized in cell-free and transient cellular expression systems, was tested for their effects on virus recovery. Four distinct plaque phenotypes were observed in cell culture: parental plaque-size (13 mutants), reduced plaque-size (17 mutants), small plaque-size (8 mutants) and no plaque-formation (8 mutants). No mutants displayed any temperature sensitivity based on recovery of virus after RNA transfection at 32 versus 37 °C. Most small plaque-mutants were defective in growth efficiency compared with parental virus. However not all small plaque-mutants had defective 2B/3 cleavage, with some showing selective defects at other non-structural protein cleavage sites. Revertant viruses were recovered for six mutations that caused reduced plaque sizes. Same-site and second-site mutations occurred in NS2B, and one second-site mutation occurred in the NS3 protease domain. Some reversion mutations ameliorated defects in cleavage activity and plaque size caused by the original mutation. These data indicate that certain mutations that reduce NS2B–NS3 protease cleavage activity cause growth restriction of yellow fever virus in cell culture. However, for at least two mutations, processing defects other than impaired cleavage activity at the 2B/3 site may account for the mutant phenotype. The existence of reversion mutations primarily in NS2B rather than NS3, suggests that the protease domain is less tolerant of structural perturbation compared with the NS2B protein.


2000 ◽  
Vol 11 (1) ◽  
pp. 15-19 ◽  
Author(s):  
Martin Katz, Zafar Shaikh, Howard I Maibac
Keyword(s):  

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