June 19, 1995FEBS LettersOpen Access

Mutations in the hydrophobic domain of poliovirus protein 3AB abrogate its permeabilizing activity

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Population

E. coli cells

Design

Preclinical

Authors

Discussion

3AB pore activity may alter host membrane permeability in poliovirus infection; leaves open its role in pathogenesis and therapeutic targeting.

Population

E. coli cells

Intervention

Expression of wild type poliovirus protein 3AB and mutants with amino acid substitutions in the hydrophobic domain

Outcome

Membrane permeability (influx and efflux of nucleosides, lactose analogues, antibiotics, and uridine)surrogate

Poliovirus protein 3AB possesses an intrinsic ability to form pores in natural membranes, allowing the flux of small hydrophilic molecules.

Lama et al. (1995) studied this question.

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3AB pore activity may alter host membrane permeability in poliovirus infection; leaves open its role in pathogenesis and therapeutic targeting.