Special Issue "Phage Assembly Pathways - To the Memory of Lindsay Black"

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Bacterial Viruses".

Deadline for manuscript submissions: 31 December 2021.

Special Issue Editors

Prof. Dr. Andreas Kuhn
E-Mail Website
Guest Editor
Institute of Microbiology and Molecular Biology, University of Hohenheim, Stuttgart, Germany
Dr. Julie Thomas
E-Mail Website
Guest Editor
Thomas H. Gosnell School of Life Sciences, College of Science, Rochester Institute of Technology, Rochester, NY, USA
Interests: giant phages; phage structure/assembly; genomics; genetics; proteomics; host–phage interactions
Special Issues and Collections in MDPI journals

Special Issue Information

Dear Colleagues,

Most fascinating in protein biochemistry are the complex assembly systems that we know from phage and virus particles. Phage assembly occurs within the prokaryotic host cell and involves replicated viral proteins and genetic material being transformed into infectious progeny. The assembly of each bacteriophage particle results from a self-triggered process that is exquisitely controlled by a series of conformational cascades. In general, the assembly process is initiated by an oligomeric protein that recruits defined partner proteins in consecutive steps creating an assembly product of increasing complexity. The driving mechanism for this process is hidden in the intrinsic conformational flexibility of each protein which drives the assembly reaction forward. Therefore, numbers of phage assembly steps have been able to be reconstituted in vitro without any energetic input from the host.

Much of what we currently know regarding phage assembly is derived from the study of the classic phage genetic systems, such as that of T4. Yet, even for such model systems there remain major unresolved questions. For example, for the many of the more recently discovered phages, there is a myriad of questions regarding how their virions assemble. To address these questions an impressive array of experimental approaches available. These include the recent advent of novel technologies such as high-resolution tomography and cryo-electron microscopy which when combined with biochemical methods allow us to follow these processes in molecular detail and possibly even at an atomic resolution.

This special issue is dedicated to Lindsay W. Black. Lindsay was a great leader in the field of phage assembly. Sadly, Lindsay passed away earlier this year. For over 40 years, Lindsay dissected the molecular processes by which the T4 head assembles in his laboratory at the University of Maryland. Using the T4 system, Lindsay became a central figure in the field of DNA packaging and he continued to make contributions to this field for most of his career. Lindsay was also fascinated by other aspects of phage assembly and replication and made significant contributions to various other areas, including virus structure, and prohead assembly and maturation.  Lindsay was a brilliant scientist and a true friend to many. To honor Lindsay’s legacy, we welcome submissions to this special issue that focuses on Lindsay’s research passion, phage assembly.

Prof. Dr. Andreas Kuhn
Dr. Julie Thomas
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Viruses is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2200 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • capsid assembly
  • DNA packaging
  • portal assembly
  • host receptor
  • tail contraction
  • ejectosome assembly
  • DNA translocation
  • lysis control

Published Papers (2 papers)

Order results
Result details
Select all
Export citation of selected articles as:

Research

Article
Intravirion DNA Can Access the Space Occupied by the Bacteriophage P22 Ejection Proteins
Viruses 2021, 13(8), 1504; https://doi.org/10.3390/v13081504 - 30 Jul 2021
Viewed by 692
Abstract
Tailed double-stranded DNA bacteriophages inject some proteins with their dsDNA during infection. Phage P22 injects about 12, 12, and 30 molecules of the proteins encoded by genes 7, 16 and 20, respectively. After their ejection from the virion, they assemble into [...] Read more.
Tailed double-stranded DNA bacteriophages inject some proteins with their dsDNA during infection. Phage P22 injects about 12, 12, and 30 molecules of the proteins encoded by genes 7, 16 and 20, respectively. After their ejection from the virion, they assemble into a trans-periplasmic conduit through which the DNA passes to enter the cytoplasm. The location of these proteins in the virion before injection is not well understood, although we recently showed they reside near the portal protein barrel in DNA-filled heads. In this report we show that when these proteins are missing from the virion, a longer than normal DNA molecule is encapsidated by the P22 headful DNA packaging machinery. Thus, the ejection proteins occupy positions within the virion that can be occupied by packaged DNA when they are absent. Full article
(This article belongs to the Special Issue Phage Assembly Pathways - To the Memory of Lindsay Black)
Show Figures

Figure 1

Article
Membrane Insertion of the M13 Minor Coat Protein G3p Is Dependent on YidC and the SecAYEG Translocase
Viruses 2021, 13(7), 1414; https://doi.org/10.3390/v13071414 - 20 Jul 2021
Viewed by 442
Abstract
The minor coat protein G3p of bacteriophage M13 is the key component for the host interaction of this virus and binds to Escherichia coli at the tip of the F pili. As we show here, during the biosynthesis of G3p as a preprotein, [...] Read more.
The minor coat protein G3p of bacteriophage M13 is the key component for the host interaction of this virus and binds to Escherichia coli at the tip of the F pili. As we show here, during the biosynthesis of G3p as a preprotein, the signal sequence interacts primarily with SecY, whereas the hydrophobic anchor sequence at the C-terminus interacts with YidC. Using arrested nascent chains and thiol crosslinking, we show here that the ribosome-exposed signal sequence is first contacted by SecY but not by YidC, suggesting that only SecYEG is involved at this early stage. The protein has a large periplasmic domain, a hydrophobic anchor sequence of 21 residues and a short C-terminal tail that remains in the cytoplasm. During the later synthesis of the entire G3p, the residues 387, 389 and 392 in anchor domain contact YidC in its hydrophobic slide to hold translocation of the C-terminal tail. Finally, the protein is processed by leader peptidase and assembled into new progeny phage particles that are extruded out of the cell. Full article
(This article belongs to the Special Issue Phage Assembly Pathways - To the Memory of Lindsay Black)
Show Figures

Figure 1

Back to TopTop