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Temperate Streptococcus thermophilus phages expressing superinfection exclusion proteins of the Ltp type

Lipoprotein Ltp encoded by temperate Streptococcus thermophilus phage TP-J34 is the prototype of the wide-spread family of host cell surface-exposed lipoproteins involved in superinfection exclusion (sie). When screening for other S. thermophilus phages expressing this type of lipoprotein, three tem...

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Autores principales: Ali, Yahya, Koberg, Sabrina, Heßner, Stefanie, Sun, Xingmin, Rabe, Björn, Back, Angela, Neve, Horst, Heller, Knut J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3952083/
https://www.ncbi.nlm.nih.gov/pubmed/24659988
http://dx.doi.org/10.3389/fmicb.2014.00098
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author Ali, Yahya
Koberg, Sabrina
Heßner, Stefanie
Sun, Xingmin
Rabe, Björn
Back, Angela
Neve, Horst
Heller, Knut J.
author_facet Ali, Yahya
Koberg, Sabrina
Heßner, Stefanie
Sun, Xingmin
Rabe, Björn
Back, Angela
Neve, Horst
Heller, Knut J.
author_sort Ali, Yahya
collection PubMed
description Lipoprotein Ltp encoded by temperate Streptococcus thermophilus phage TP-J34 is the prototype of the wide-spread family of host cell surface-exposed lipoproteins involved in superinfection exclusion (sie). When screening for other S. thermophilus phages expressing this type of lipoprotein, three temperate phages—TP-EW, TP-DSM20617, and TP-778—were isolated. In this communication we present the total nucleotide sequences of TP-J34 and TP-778L. For TP-EW, a phage almost identical to TP-J34, besides the ltp gene only the two regions of deviation from TP-J34 DNA were analyzed: the gene encoding the tail protein causing an assembly defect in TP-J34 and the gene encoding the lysin, which in TP-EW contains an intron. For TP-DSM20617 only the sequence of the lysogeny module containing the ltp gene was determined. The region showed high homology to the same region of TP-778. For TP-778 we could show that absence of the attR region resulted in aberrant excision of phage DNA. The amino acid sequence of mature Ltp(TP-EW) was shown to be identical to that of mature Ltp(TP-J34), whereas the amino acid sequence of mature Ltp(TP-778) was shown to differ from mature Ltp(TP-J34) in eight amino acid positions. Ltp(TP-DSM20617) was shown to differ from Ltp(TP-778) in just one amino acid position. In contrast to Ltp(TP-J34), Ltp(TP-778) did not affect infection of lactococcal phage P008 instead increased activity against phage P001 was noticed.
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spelling pubmed-39520832014-03-21 Temperate Streptococcus thermophilus phages expressing superinfection exclusion proteins of the Ltp type Ali, Yahya Koberg, Sabrina Heßner, Stefanie Sun, Xingmin Rabe, Björn Back, Angela Neve, Horst Heller, Knut J. Front Microbiol Microbiology Lipoprotein Ltp encoded by temperate Streptococcus thermophilus phage TP-J34 is the prototype of the wide-spread family of host cell surface-exposed lipoproteins involved in superinfection exclusion (sie). When screening for other S. thermophilus phages expressing this type of lipoprotein, three temperate phages—TP-EW, TP-DSM20617, and TP-778—were isolated. In this communication we present the total nucleotide sequences of TP-J34 and TP-778L. For TP-EW, a phage almost identical to TP-J34, besides the ltp gene only the two regions of deviation from TP-J34 DNA were analyzed: the gene encoding the tail protein causing an assembly defect in TP-J34 and the gene encoding the lysin, which in TP-EW contains an intron. For TP-DSM20617 only the sequence of the lysogeny module containing the ltp gene was determined. The region showed high homology to the same region of TP-778. For TP-778 we could show that absence of the attR region resulted in aberrant excision of phage DNA. The amino acid sequence of mature Ltp(TP-EW) was shown to be identical to that of mature Ltp(TP-J34), whereas the amino acid sequence of mature Ltp(TP-778) was shown to differ from mature Ltp(TP-J34) in eight amino acid positions. Ltp(TP-DSM20617) was shown to differ from Ltp(TP-778) in just one amino acid position. In contrast to Ltp(TP-J34), Ltp(TP-778) did not affect infection of lactococcal phage P008 instead increased activity against phage P001 was noticed. Frontiers Media S.A. 2014-03-13 /pmc/articles/PMC3952083/ /pubmed/24659988 http://dx.doi.org/10.3389/fmicb.2014.00098 Text en Copyright © 2014 Ali, Koberg, Heßner, Sun, Rabe, Back, Neve and Heller. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Ali, Yahya
Koberg, Sabrina
Heßner, Stefanie
Sun, Xingmin
Rabe, Björn
Back, Angela
Neve, Horst
Heller, Knut J.
Temperate Streptococcus thermophilus phages expressing superinfection exclusion proteins of the Ltp type
title Temperate Streptococcus thermophilus phages expressing superinfection exclusion proteins of the Ltp type
title_full Temperate Streptococcus thermophilus phages expressing superinfection exclusion proteins of the Ltp type
title_fullStr Temperate Streptococcus thermophilus phages expressing superinfection exclusion proteins of the Ltp type
title_full_unstemmed Temperate Streptococcus thermophilus phages expressing superinfection exclusion proteins of the Ltp type
title_short Temperate Streptococcus thermophilus phages expressing superinfection exclusion proteins of the Ltp type
title_sort temperate streptococcus thermophilus phages expressing superinfection exclusion proteins of the ltp type
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3952083/
https://www.ncbi.nlm.nih.gov/pubmed/24659988
http://dx.doi.org/10.3389/fmicb.2014.00098
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