Mechanism of adsorption and eclipse of bacteriophage phi X174. I. In vitro conformational change under conditions of eclipse.
Bacteriophage phiX174 undergoes a conformational change during viral eclipse when virus-host cell complexes are incubated briefly at 37 C in a complex starvation buffer at pH 8. In this report, basically the same transition is demonstrated in vitro. Incubation of phiX alone for 2 to 3 hr at 35 C in 0.1 m CaCl(2) (pH 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 pH 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 phiX.
D000327:Adsorption; D002021:Buffers; D002118:Calcium / Q000378:metabolism; D002499:Centrifugation, Density Gradient; D002586:Cesium; D002712:Chlorides; D002850:Chromatography, Gel; D003090:Coliphages / Q000254:growth & development / Q000302:isolation & purification / Q000378:metabolism*; D004926:Escherichia coli; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D013395:Sucrose; D013696:Temperature; D013997:Time Factors; D014461:Ultracentrifugation
D002021:Buffers; D002712:Chlorides; D002586:Cesium; D013395:Sucrose; D002118:Calcium