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Viruses 2016, 8(1), 26; doi:10.3390/v8010026

Branched Lateral Tail Fiber Organization in T5-Like Bacteriophages DT57C and DT571/2 is Revealed by Genetic and Functional Analysis

1
Winogradsky Institute of Microbiology, Research Center of Biotechnology of the Russian Academy of Sciences, Leninsky Ave. 33, build. 2, Moscow 119071, Russia
2
Moscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, 141700, Russia
3
École Polytechnique Fédérale de Lausanne (EPFL), BSP-415, 1015 Lausanne, Switzerland
4
N. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky Ave. 47, Moscow 119991, Russia
5
Federal Research and Clinical Center of Physical-Chemical Medicine of Federal Medical Biological Agency, Pirogovskaya ul., 1a, Moscow 119435, Russia
6
A.N. Severtsov Institute of Ecology and Evolution, Biotechnology of the Russian Academy of Sciences, Leninsky Ave. 33, build. 2, Moscow 119071, Russia
*
Author to whom correspondence should be addressed.
Academic Editors: Abram Aertsen and Rob Lavigne
Received: 12 September 2015 / Revised: 14 December 2015 / Accepted: 11 January 2016 / Published: 21 January 2016
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Abstract

The T5-like siphoviruses DT57C and DT571/2, isolated from horse feces, are very closely related to each other, and most of their structural proteins are also nearly identical to T5 phage. Their LTFs (L-shaped tail fibers), however, are composed of two proteins, LtfA and LtfB, instead of the single Ltf of bacteriophage T5. In silico and mutant analysis suggests a possible branched structure of DT57C and DT571/2 LTFs, where the LtfB protein is connected to the phage tail via the LtfA protein and with both proteins carrying receptor recognition domains. Such adhesin arrangement has not been previously recognized in siphoviruses. The LtfA proteins of our phages are found to recognize different host O-antigen types: E. coli O22-like for DT57C phage and E. coli O87 for DT571/2. LtfB proteins are identical in both phages and recognize another host receptor, most probably lipopolysaccharide (LPS) of E. coli O81 type. In these two bacteriophages, LTF function is essential to penetrate the shield of the host’s O-antigens. We also demonstrate that LTF-mediated adsorption becomes superfluous when the non-specific cell protection by O-antigen is missing, allowing the phages to bind directly to their common secondary receptor, the outer membrane protein BtuB. The LTF independent adsorption was also demonstrated on an O22-like host mutant missing O-antigen O-acetylation, thus showing the biological value of this O-antigen modification for cell protection against phages. View Full-Text
Keywords: bacteriophage; T5-like phage; bacteriophage adsorption; phage in situ evolution; tail fiber proteins; phage branched adhesin; E. coli O-antigen; O-antigen O-acetylation; horse feces bacteriophage; T5-like phage; bacteriophage adsorption; phage in situ evolution; tail fiber proteins; phage branched adhesin; E. coli O-antigen; O-antigen O-acetylation; horse feces
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Golomidova, A.K.; Kulikov, E.E.; Prokhorov, N.S.; Guerrero-Ferreira, R.С.; Knirel, Y.A.; Kostryukova, E.S.; Tarasyan, K.K.; Letarov, A.V. Branched Lateral Tail Fiber Organization in T5-Like Bacteriophages DT57C and DT571/2 is Revealed by Genetic and Functional Analysis. Viruses 2016, 8, 26.

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