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Title: Three-dimensional reconstructions of the bacteriophage CUS-3 virion reveal a conserved coat protein I-domain but a distinct tailspike receptor-binding domain

Abstract

CUS-3 is a short-tailed, dsDNA bacteriophage that infects serotype K1 Escherichia coli. We report icosahedrally averaged and asymmetric, three-dimensional, cryo-electron microscopic reconstructions of the CUS-3 virion. Its coat protein structure adopts the “HK97-fold” shared by other tailed phages and is quite similar to that in phages P22 and Sf6 despite only weak amino acid sequence similarity. In addition, these coat proteins share a unique extra external domain (“I-domain”), suggesting that the group of P22-like phages has evolved over a very long time period without acquiring a new coat protein gene from another phage group. On the other hand, the morphology of the CUS-3 tailspike differs significantly from that of P22 or Sf6, but is similar to the tailspike of phage K1F, a member of the extremely distantly related T7 group of phages. We conclude that CUS-3 obtained its tailspike gene from a distantly related phage quite recently. - Highlights: • Asymmetric and symmetric three-dimensional reconstructions of phage CUS-3 are presented. • CUS-3 major capsid protein has a conserved I-domain, which is found in all three categories of “P22-like phage”. • CUS-3 has very different tailspike receptor binding domain from those of P22 and Sf6. • The CUS-3 tailspike likely wasmore » acquired by horizontal gene transfer.« less

Authors:
 [1]; ;  [1];  [2]; ;  [1];  [2];  [1];  [3]
  1. Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0378 (United States)
  2. University of Utah School of Medicine, Division of Microbiology and Immunology, Department of Pathology, Salt Lake City, UT 84112 (United States)
  3. (United States)
Publication Date:
OSTI Identifier:
22435053
Resource Type:
Journal Article
Journal Name:
Virology
Additional Journal Information:
Journal Volume: 464-465; Other Information: Copyright (c) 2014 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0042-6822
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; AMINO ACID SEQUENCE; ASYMMETRY; BACTERIOPHAGES; ELECTRON MICROSCOPY; ESCHERICHIA COLI; GENES; MORPHOLOGY; PROTEIN STRUCTURE; RECEPTORS; SYMMETRY; THREE-DIMENSIONAL CALCULATIONS

Citation Formats

Parent, Kristin N., E-mail: kparent@msu.edu, Tang, Jinghua, Cardone, Giovanni, Gilcrease, Eddie B., Janssen, Mandy E., Olson, Norman H., Casjens, Sherwood R., E-mail: sherwood.casjens@path.utah.edu, Baker, Timothy S., E-mail: tsb@ucsd.edu, and University of California, San Diego, Division of Biological Sciences, La Jolla, CA, 92093. Three-dimensional reconstructions of the bacteriophage CUS-3 virion reveal a conserved coat protein I-domain but a distinct tailspike receptor-binding domain. United States: N. p., 2014. Web. doi:10.1016/J.VIROL.2014.06.017.
Parent, Kristin N., E-mail: kparent@msu.edu, Tang, Jinghua, Cardone, Giovanni, Gilcrease, Eddie B., Janssen, Mandy E., Olson, Norman H., Casjens, Sherwood R., E-mail: sherwood.casjens@path.utah.edu, Baker, Timothy S., E-mail: tsb@ucsd.edu, & University of California, San Diego, Division of Biological Sciences, La Jolla, CA, 92093. Three-dimensional reconstructions of the bacteriophage CUS-3 virion reveal a conserved coat protein I-domain but a distinct tailspike receptor-binding domain. United States. doi:10.1016/J.VIROL.2014.06.017.
Parent, Kristin N., E-mail: kparent@msu.edu, Tang, Jinghua, Cardone, Giovanni, Gilcrease, Eddie B., Janssen, Mandy E., Olson, Norman H., Casjens, Sherwood R., E-mail: sherwood.casjens@path.utah.edu, Baker, Timothy S., E-mail: tsb@ucsd.edu, and University of California, San Diego, Division of Biological Sciences, La Jolla, CA, 92093. Mon . "Three-dimensional reconstructions of the bacteriophage CUS-3 virion reveal a conserved coat protein I-domain but a distinct tailspike receptor-binding domain". United States. doi:10.1016/J.VIROL.2014.06.017.
@article{osti_22435053,
title = {Three-dimensional reconstructions of the bacteriophage CUS-3 virion reveal a conserved coat protein I-domain but a distinct tailspike receptor-binding domain},
author = {Parent, Kristin N., E-mail: kparent@msu.edu and Tang, Jinghua and Cardone, Giovanni and Gilcrease, Eddie B. and Janssen, Mandy E. and Olson, Norman H. and Casjens, Sherwood R., E-mail: sherwood.casjens@path.utah.edu and Baker, Timothy S., E-mail: tsb@ucsd.edu and University of California, San Diego, Division of Biological Sciences, La Jolla, CA, 92093},
abstractNote = {CUS-3 is a short-tailed, dsDNA bacteriophage that infects serotype K1 Escherichia coli. We report icosahedrally averaged and asymmetric, three-dimensional, cryo-electron microscopic reconstructions of the CUS-3 virion. Its coat protein structure adopts the “HK97-fold” shared by other tailed phages and is quite similar to that in phages P22 and Sf6 despite only weak amino acid sequence similarity. In addition, these coat proteins share a unique extra external domain (“I-domain”), suggesting that the group of P22-like phages has evolved over a very long time period without acquiring a new coat protein gene from another phage group. On the other hand, the morphology of the CUS-3 tailspike differs significantly from that of P22 or Sf6, but is similar to the tailspike of phage K1F, a member of the extremely distantly related T7 group of phages. We conclude that CUS-3 obtained its tailspike gene from a distantly related phage quite recently. - Highlights: • Asymmetric and symmetric three-dimensional reconstructions of phage CUS-3 are presented. • CUS-3 major capsid protein has a conserved I-domain, which is found in all three categories of “P22-like phage”. • CUS-3 has very different tailspike receptor binding domain from those of P22 and Sf6. • The CUS-3 tailspike likely was acquired by horizontal gene transfer.},
doi = {10.1016/J.VIROL.2014.06.017},
journal = {Virology},
issn = {0042-6822},
number = ,
volume = 464-465,
place = {United States},
year = {2014},
month = {9}
}