title: Mechanism of the long tail-fiber deployment of bacteriophages T-even and its role in adsorption, infection and sedimentation.
abstract: Models for the tail-fiber deployment of T-even bacteriophages have been experimentally tested by correlating sedimentation constants, adsorption rates, protease inactivation kinetics, and fiber configurations of individual phages observed by electron microscopy. Neither the collective nor the individualistic model, i.e. coordinated fiber retraction and expansion or oscillation of fibers independently of each other, respectively, could satisfactorily account for the results presented. We propose a new intermediary model, in which the base-plate determines a collective behaviour by fixing the hinge angle, around which individual fibers oscillate freely. The bidisperse, so-called dual sedimentation was shown to occur mainly with nascent high-concentration phage stocks in potassium glutamate containing media. Indeed, when mature intracellular phages are released in 0.5 M potassium glutamate--a condition simulating the intracellular environment--only the fast form appears. Upon storage in the cold or release into 0.5 M chloride, both forms appear. Results confirming that the sedimentation constants of the fast and slow form roughly correspond to those of the monodisperse sedimentation, characteristic of the extreme pH values, i.e. 5 and 8, do not allow to conclude that fiber configuration is the only cause of the bidisperse sedimentation.
authors.affiliation: Department of Microbiology, Biozentrum of the University of Basel, Switzerland.
authors.forename: E
authors.initials: E
authors.lastname: Kellenberger
authors.forename: E
authors.initials: E
authors.lastname: Stauffer
authors.forename: M
authors.initials: M
authors.lastname: Häner
authors.forename: A
authors.initials: A
authors.lastname: Lustig
authors.forename: D
authors.initials: D
authors.lastname: Karamata
mesh_terms: D000327:Adsorption; D002499:Centrifugation, Density Gradient; D003470:Culture Media; D010450:Endopeptidases / Q000494:pharmacology; D004926:Escherichia coli / Q000648:ultrastructure / Q000821:virology; D005557:Formaldehyde; D005971:Glutamates / Q000494:pharmacology; D005976:Glutaral / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008854:Microscopy, Electron; D013395:Sucrose; D013604:T-Phages / Q000737:chemistry* / Q000502:physiology / Q000648:ultrastructure; D014461:Ultracentrifugation; D017376:Viral Tail Proteins / Q000737:chemistry* / Q000648:ultrastructure
chemical_list: D003470:Culture Media; D005971:Glutamates; D017376:Viral Tail Proteins; D005557:Formaldehyde; D013395:Sucrose; D010450:Endopeptidases; D005976:Glutaral