Mechanism of Adsorption and Eclipse of Bacteriophage φX174 I. In Vitro Conformational Change Under Conditions of Eclipse

Author:

Incardona Nino L.12,Blonski Ronald12,Feeney William12

Affiliation:

1. Department of Chemistry and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306

2. Mellon Institute, Pittsburgh, Pennsylvania

Abstract

Bacteriophage φX174 undergoes a conformational change during viral eclipse when virus-host cell complexes are incubated briefly at 37 C in a complex starvation buffer at p H 8. In this report, basically the same transition is demonstrated in vitro. Incubation of φX alone for 2 to 3 hr at 35 C in 0.1 m CaCl 2 ( p H 7.2) results in an irreversible decrease in S 20,w because of an increase in the frictional coefficient that occurs during the change in conformation. The slower sedimenting conformation is noninfectious. These properties are remarkably similar to those of the eclipsed particles characterized by Newbold and Sinsheimer. Therefore, the key structural requirements for the molecular mechanism must reside within the architecture of the virus itself. This extremely simplified system uncovered the calcium ion requirement and pronounced dependence on p H between 6 and 7, both inherent properties of adsorption. This and the more than 10-fold greater rate of the in vivo conformational transition allude to the cooperative nature of attachment and eclipse for φX.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Reference21 articles.

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3. Molecular weight and other biophysical properties of bromegrass mosaic virus;Bockstahler L. E.;Biophys. J.,1962

4. Mode of host cell penetration by bacteriophage #3X174;Brown D. T.;J. Virol.,1971

5. Studies on the proteins of OX174. 11. The protein composition of the 9X174 coat;Burgess A. B.;Proc. Nat. Acad. Sci. U.S.A.,1969

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