1983
DOI: 10.1002/j.1460-2075.1983.tb01433.x
|View full text |Cite
|
Sign up to set email alerts
|

Degrees of relatedness of T-even type E. coli phages using different or the same receptors and topology of serologically cross-reacting sites.

Abstract: The relatedness of a series of T‐even like phages which use the Escherichia coli outer membrane protein OmpA as a receptor, and the classical phages T2, T4 and T6 has been investigated. Immunoelectron microscopy and the pattern of phage resistance in bacterial mutants revealed that: (i) phages of this morphology do not necessarily cross‐react serologically; (ii) phages using different receptors may bind heterologous IgG everywhere except to the tip (comprising approximately 10% of one fiber polypeptide) of the… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

0
31
0

Year Published

1985
1985
2011
2011

Publication Types

Select...
8
1

Relationship

1
8

Authors

Journals

citations
Cited by 53 publications
(31 citation statements)
references
References 44 publications
(30 reference statements)
0
31
0
Order By: Relevance
“…Double infection of a bacterial host by different phages and homologue recombination or incorrect excision and packaging of the phage DNA may lead to the transfer of DNA fragments of different origin. This is discussed as a fundamental idea for a model of modular evolution for viruses (Kim & Davidson 1974, Mise 1976, Schwarz et al 1983, Gibbs 1987, Jarvis 1995.…”
Section: Discussionmentioning
confidence: 99%
“…Double infection of a bacterial host by different phages and homologue recombination or incorrect excision and packaging of the phage DNA may lead to the transfer of DNA fragments of different origin. This is discussed as a fundamental idea for a model of modular evolution for viruses (Kim & Davidson 1974, Mise 1976, Schwarz et al 1983, Gibbs 1987, Jarvis 1995.…”
Section: Discussionmentioning
confidence: 99%
“…However, nothing is known, so far, about gp34 and gp36. Reinspection of electron micrographs, taken previously to study the serological relationships of different phages [12], reveals that monovalent antibody fragments (Fab) always bind pairwise to the regions of the tail fiber where gp34, 36 and 37 are located ( fig.4). Hence, dimerization of gp34 and 36 also occurs in a parallel fashion.…”
Section: Volume 215 Number L Febs Letters May 1987mentioning
confidence: 99%
“…Electron microscopy. Phage Tull*-46 is shown with antibodies against phage Tull*-6 [12]. Monovalent antibody fragments (Fab) (arrowheads) bind always pairwise to regions including gp34, 36 and 37.…”
Section: Model For the Fiber Structurementioning
confidence: 99%
“…This leads to a conformational change in the base plate structure and unfolding of the short tail fibers that bind irreversibly to LPS moieties, resulting in contraction of the tail sheath and DNA injection (41,58). Other outer membrane proteins such as OmpA and OmpF also serve as receptors for members of the T-even group, and several of these Omp-specific phages also rely on specific structures in the LPS for infectivity in addition to the porin as seen for T4 (33,34,45,58). Phages recognizing capsular polysaccharides have also been described for E. coli, and these phages not only bind but also cleave their receptor in order to get into contact with the host membrane for injection of their DNA (48).…”
mentioning
confidence: 99%