June 1, 1995Journal of VirologyOpen Access

The rubella virus RNA binding activity of human calreticulin is localized to the N-terminal domain

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Population

Recombinant human calreticulin expressed in E. coli as a fusion protein with maltose-binding protein and its…

Comparison

N-terminal deletions and domain isolations of… vs Full-length calreticulin or MBP alone

Design

Preclinical

Authors

Discussion

Localizes rubella activities to calreticulin N-terminal domains; leaves open targeted antiviral strategies pending human validation.

Population

Recombinant human calreticulin expressed in E. coli as a fusion protein with maltose-binding protein (MBP-Cal) and its truncated derivatives

Intervention

N-terminal deletions and domain isolations of calreticulin

Comparator

Full-length calreticulin or MBP alone

Outcome

RNA-binding activity to rubella virus RNA 3' cis-acting element and autophosphorylation activity

Both the rubella virus RNA-binding and autophosphorylation activities of human calreticulin are localized to its N-terminal domain.

Atreya et al. (1995) studied this question.

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