April 1, 1997Journal of VirologyOpen Access

Proteinase 3C-mediated processing of VP1-2A of two hepatitis A virus strains: in vivo evidence for cleavage at amino acid position 273/274 of VP1

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Population

in vivo expression system for hepatitis A virus (HAV) strains, including the attenuated HM175 strain

Design

Preclinical

Authors

CPChristian ProbstFundação Carlos Chagas MJMonika JechtUniversity of Lübeck VGVerena Gauss‐MüllerUniversity of Lübeck

Discussion

Member takes

Implication

VP1 cleavage efficiency by 3Cpro may underlie strain attenuation; leaves open relevance to human HAV pathogenesis or vaccines.

Structured PICO

Population

in vivo expression system for hepatitis A virus (HAV) strains, including the attenuated HM175 strain

Intervention

Proteinase 3Cpro-mediated processing

Outcome

Proteolytic liberation of VP1 from its precursors P1-2A and VP1-2A

The study demonstrates that HAV proteinase 3Cpro catalyzes the cleavage of VP1 from its precursors, with strain-specific differences in cleavage efficiency at position 273/274.

Cite This Study

Probst et al. (1997) studied this question.

synapsesocial.com/papers/6a891db06abbd4965f28b34d https://doi.org/10.1128/jvi.71.4.3288-3292.1997

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April 1, 1997Journal of VirologyOpen Access

Proteinase 3C-mediated processing of VP1-2A of two hepatitis A virus strains: in vivo evidence for cleavage at amino acid position 273/274 of VP1

View Full Paper

Ask AI

Bookmark

Population

in vivo expression system for hepatitis A virus (HAV) strains, including the attenuated HM175 strain

Design

Preclinical

Authors

CPChristian ProbstFundação Carlos Chagas MJMonika JechtUniversity of Lübeck VGVerena Gauss‐MüllerUniversity of Lübeck

Discussion

Member takes

Implication

VP1 cleavage efficiency by 3Cpro may underlie strain attenuation; leaves open relevance to human HAV pathogenesis or vaccines.

Structured PICO

Population

in vivo expression system for hepatitis A virus (HAV) strains, including the attenuated HM175 strain

Intervention

Proteinase 3Cpro-mediated processing

Outcome

Proteolytic liberation of VP1 from its precursors P1-2A and VP1-2A

The study demonstrates that HAV proteinase 3Cpro catalyzes the cleavage of VP1 from its precursors, with strain-specific differences in cleavage efficiency at position 273/274.

Cite This Study

Probst et al. (1997) studied this question.

synapsesocial.com/papers/6a891db06abbd4965f28b34d https://doi.org/10.1128/jvi.71.4.3288-3292.1997

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