In silico analysis of AHJD‐like viruses, Staphylococcus aureus phages S24‐1 and S13′, and study of phage S24‐1 adsorption. Issue 2 (4th March 2014)
- Record Type:
- Journal Article
- Title:
- In silico analysis of AHJD‐like viruses, Staphylococcus aureus phages S24‐1 and S13′, and study of phage S24‐1 adsorption. Issue 2 (4th March 2014)
- Main Title:
- In silico analysis of AHJD‐like viruses, Staphylococcus aureus phages S24‐1 and S13′, and study of phage S24‐1 adsorption
- Authors:
- Uchiyama, Jumpei
Takemura‐Uchiyama, Iyo
Kato, Shin‐ichiro
Sato, Miho
Ujihara, Takako
Matsui, Hidehito
Hanaki, Hideaki
Daibata, Masanori
Matsuzaki, Shigenobu - Abstract:
- <abstract abstract-type="main" id="mbo3166-abs-0001"> <title>Abstract</title> <p> <italic>Staphylococcus aureus</italic> is a clinically important bacterium that is commensal in both humans and animals. Bacteriophage (phage) attachment to the host bacterial surface is an important process during phage infection, which involves interactions between phage receptor‐binding proteins and host receptor molecules. However, little information is available on the receptor‐binding protein of <italic>S. aureus</italic> phages. <italic>S. aureus</italic> virulent phages S24‐1 and S13′ (family <italic>Podoviridae</italic>, genus AHJD‐like viruses) were isolated from sewage. In the present study, we investigated the receptor‐binding protein of AHJD‐like viruses using phage S24‐1. First, based on a comparative genomic analysis of phages S24‐1 and S13′, open reading frame 16 (ORF16) of phage S24‐1 was speculated to be the receptor‐binding protein, which possibly determines the host range. Second, we demonstrated that this was the receptor‐binding protein of phage S24‐1. Third, our study suggested that wall teichoic acids in the cell walls of <italic>S. aureus</italic> are the main receptor molecules for ORF16 and phage S24‐1. Finally, the C‐terminal region of ORF16 may be essential for binding to <italic>S. aureus</italic>. These results strongly suggest that ORF16 of phage S24‐1 and its homologs may be the receptor‐binding proteins of AHJD‐like viruses.</p> </abstract>
- Is Part Of:
- MicrobiologyOpen. Volume 3:Issue 2(2014:Apr.)
- Journal:
- MicrobiologyOpen
- Issue:
- Volume 3:Issue 2(2014:Apr.)
- Issue Display:
- Volume 3, Issue 2 (2014)
- Year:
- 2014
- Volume:
- 3
- Issue:
- 2
- Issue Sort Value:
- 2014-0003-0002-0000
- Page Start:
- 257
- Page End:
- 270
- Publication Date:
- 2014-03-04
- Subjects:
- Microbiology -- Periodicals
579 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)2045-8827 ↗ - DOI:
- 10.1002/mbo3.166 ↗
- Languages:
- English
- ISSNs:
- 2045-8827
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3094.xml