Capsular polysaccharide is a receptor of a clostridium perfringens bacteriophage CPS1

Eunsu Ha, Jihwan Chun, Minsik Kim, Sangryeo Ryu

Research output: Contribution to journalArticle

Abstract

Clostridium perfringens is a Gram-positive, anaerobic, and spore forming bacterium that is widely distributed in the environment and one of the most common causes of foodborne illnesses. Bacteriophages are regarded as one of the most promising alternatives to antibiotics in controlling antibiotic-resistant pathogenic bacteria. Here we isolated a virulent C. perfringens phage, CPS1, and analysis of its whole genome and morphology revealed a small genome (19 kbps) and a short noncontractile tail, suggesting that CPS1 can be classified as a member of Picovirinae, a subfamily of Podoviridae. To determine the host receptor of CPS1, the EZ-Tn5 random transposon mutant library of C. perfringens ATCC 13124 was constructed and screened for resistance to CPS1 infection. Analysis of the CPS1-resistant mutants revealed that the CPF_0486 was disrupted by Tn5. The CPF_0486 was annotated as galE, a gene encoding UDP-glucose 4-epimerase (GalE). However, biochemical analyses demonstrated that the encoded protein possessed dual activities of GalE and UDP-N-acetylglucosamine 4-epimerase (Gne). We found that the CPF_0486::Tn5 mutant produced a reduced amount of capsular polysaccharides (CPS) compared with the wild type. We also discovered that glucosamine and galactosamine could competitively inhibit host adsorption of CPS1. These results suggest that CPS acts as a receptor for this phage.

Original languageEnglish
Article number1002
JournalViruses
Volume11
Issue number11
DOIs
Publication statusPublished - 2019 Oct 31

Fingerprint

Clostridium perfringens
Bacteriophages
Polysaccharides
Podoviridae
UDPglucose 4-Epimerase
Genome
Anti-Bacterial Agents
Bacteria
Virus Receptors
Galactosamine
Foodborne Diseases
Glucosamine
Spores
Adsorption
Infection
Genes
Proteins

All Science Journal Classification (ASJC) codes

  • Infectious Diseases
  • Virology

Cite this

Ha, Eunsu ; Chun, Jihwan ; Kim, Minsik ; Ryu, Sangryeo. / Capsular polysaccharide is a receptor of a clostridium perfringens bacteriophage CPS1. In: Viruses. 2019 ; Vol. 11, No. 11.
@article{7cc82cc5cbfc47a98089c0ab8e9c7dcf,
title = "Capsular polysaccharide is a receptor of a clostridium perfringens bacteriophage CPS1",
abstract = "Clostridium perfringens is a Gram-positive, anaerobic, and spore forming bacterium that is widely distributed in the environment and one of the most common causes of foodborne illnesses. Bacteriophages are regarded as one of the most promising alternatives to antibiotics in controlling antibiotic-resistant pathogenic bacteria. Here we isolated a virulent C. perfringens phage, CPS1, and analysis of its whole genome and morphology revealed a small genome (19 kbps) and a short noncontractile tail, suggesting that CPS1 can be classified as a member of Picovirinae, a subfamily of Podoviridae. To determine the host receptor of CPS1, the EZ-Tn5 random transposon mutant library of C. perfringens ATCC 13124 was constructed and screened for resistance to CPS1 infection. Analysis of the CPS1-resistant mutants revealed that the CPF_0486 was disrupted by Tn5. The CPF_0486 was annotated as galE, a gene encoding UDP-glucose 4-epimerase (GalE). However, biochemical analyses demonstrated that the encoded protein possessed dual activities of GalE and UDP-N-acetylglucosamine 4-epimerase (Gne). We found that the CPF_0486::Tn5 mutant produced a reduced amount of capsular polysaccharides (CPS) compared with the wild type. We also discovered that glucosamine and galactosamine could competitively inhibit host adsorption of CPS1. These results suggest that CPS acts as a receptor for this phage.",
author = "Eunsu Ha and Jihwan Chun and Minsik Kim and Sangryeo Ryu",
year = "2019",
month = "10",
day = "31",
doi = "10.3390/v11111005",
language = "English",
volume = "11",
journal = "Viruses",
issn = "1999-4915",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "11",

}

Capsular polysaccharide is a receptor of a clostridium perfringens bacteriophage CPS1. / Ha, Eunsu; Chun, Jihwan; Kim, Minsik; Ryu, Sangryeo.

In: Viruses, Vol. 11, No. 11, 1002, 31.10.2019.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Capsular polysaccharide is a receptor of a clostridium perfringens bacteriophage CPS1

AU - Ha, Eunsu

AU - Chun, Jihwan

AU - Kim, Minsik

AU - Ryu, Sangryeo

PY - 2019/10/31

Y1 - 2019/10/31

N2 - Clostridium perfringens is a Gram-positive, anaerobic, and spore forming bacterium that is widely distributed in the environment and one of the most common causes of foodborne illnesses. Bacteriophages are regarded as one of the most promising alternatives to antibiotics in controlling antibiotic-resistant pathogenic bacteria. Here we isolated a virulent C. perfringens phage, CPS1, and analysis of its whole genome and morphology revealed a small genome (19 kbps) and a short noncontractile tail, suggesting that CPS1 can be classified as a member of Picovirinae, a subfamily of Podoviridae. To determine the host receptor of CPS1, the EZ-Tn5 random transposon mutant library of C. perfringens ATCC 13124 was constructed and screened for resistance to CPS1 infection. Analysis of the CPS1-resistant mutants revealed that the CPF_0486 was disrupted by Tn5. The CPF_0486 was annotated as galE, a gene encoding UDP-glucose 4-epimerase (GalE). However, biochemical analyses demonstrated that the encoded protein possessed dual activities of GalE and UDP-N-acetylglucosamine 4-epimerase (Gne). We found that the CPF_0486::Tn5 mutant produced a reduced amount of capsular polysaccharides (CPS) compared with the wild type. We also discovered that glucosamine and galactosamine could competitively inhibit host adsorption of CPS1. These results suggest that CPS acts as a receptor for this phage.

AB - Clostridium perfringens is a Gram-positive, anaerobic, and spore forming bacterium that is widely distributed in the environment and one of the most common causes of foodborne illnesses. Bacteriophages are regarded as one of the most promising alternatives to antibiotics in controlling antibiotic-resistant pathogenic bacteria. Here we isolated a virulent C. perfringens phage, CPS1, and analysis of its whole genome and morphology revealed a small genome (19 kbps) and a short noncontractile tail, suggesting that CPS1 can be classified as a member of Picovirinae, a subfamily of Podoviridae. To determine the host receptor of CPS1, the EZ-Tn5 random transposon mutant library of C. perfringens ATCC 13124 was constructed and screened for resistance to CPS1 infection. Analysis of the CPS1-resistant mutants revealed that the CPF_0486 was disrupted by Tn5. The CPF_0486 was annotated as galE, a gene encoding UDP-glucose 4-epimerase (GalE). However, biochemical analyses demonstrated that the encoded protein possessed dual activities of GalE and UDP-N-acetylglucosamine 4-epimerase (Gne). We found that the CPF_0486::Tn5 mutant produced a reduced amount of capsular polysaccharides (CPS) compared with the wild type. We also discovered that glucosamine and galactosamine could competitively inhibit host adsorption of CPS1. These results suggest that CPS acts as a receptor for this phage.

UR - http://www.scopus.com/inward/record.url?scp=85074548545&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85074548545&partnerID=8YFLogxK

U2 - 10.3390/v11111005

DO - 10.3390/v11111005

M3 - Article

C2 - 31683584

AN - SCOPUS:85074548545

VL - 11

JO - Viruses

JF - Viruses

SN - 1999-4915

IS - 11

M1 - 1002

ER -