Cargando…
Structure and Function of Hoc—A Novel Environment Sensing Device Encoded by T4 and Other Bacteriophages
Bacteriophage T4 is decorated with 155 180 Å-long fibers of the highly antigenic outer capsid protein (Hoc). In this study, we describe a near-atomic structural model of Hoc by combining cryo-electron microscopy and AlphaFold structure predictions. It consists of a conserved C-terminal capsid-bindin...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10385173/ https://www.ncbi.nlm.nih.gov/pubmed/37515203 http://dx.doi.org/10.3390/v15071517 |
_version_ | 1785081339515502592 |
---|---|
author | Fokine, Andrei Islam, Mohammad Zahidul Fang, Qianglin Chen, Zhenguo Sun, Lei Rao, Venigalla B. |
author_facet | Fokine, Andrei Islam, Mohammad Zahidul Fang, Qianglin Chen, Zhenguo Sun, Lei Rao, Venigalla B. |
author_sort | Fokine, Andrei |
collection | PubMed |
description | Bacteriophage T4 is decorated with 155 180 Å-long fibers of the highly antigenic outer capsid protein (Hoc). In this study, we describe a near-atomic structural model of Hoc by combining cryo-electron microscopy and AlphaFold structure predictions. It consists of a conserved C-terminal capsid-binding domain attached to a string of three variable immunoglobulin (Ig)-like domains, an architecture well-preserved in hundreds of Hoc molecules found in phage genomes. Each T4-Hoc fiber attaches randomly to the center of gp23* hexameric capsomers in one of the six possible orientations, though at the vertex-proximal hexamers that deviate from 6-fold symmetry, Hoc binds in two preferred orientations related by 180° rotation. Remarkably, each Hoc fiber binds to all six subunits of the capsomer, though the interactions are greatest with three of the subunits, resulting in the off-centered attachment of the C-domain. Biochemical analyses suggest that the acidic Hoc fiber (pI, ~4–5) allows for the clustering of virions in acidic pH and dispersion in neutral/alkaline pH. Hoc appears to have evolved as a sensing device that allows the phage to navigate its movements through reversible clustering–dispersion transitions so that it reaches its destination, the host bacterium, and persists in various ecological niches such as the human/mammalian gut. |
format | Online Article Text |
id | pubmed-10385173 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-103851732023-07-30 Structure and Function of Hoc—A Novel Environment Sensing Device Encoded by T4 and Other Bacteriophages Fokine, Andrei Islam, Mohammad Zahidul Fang, Qianglin Chen, Zhenguo Sun, Lei Rao, Venigalla B. Viruses Article Bacteriophage T4 is decorated with 155 180 Å-long fibers of the highly antigenic outer capsid protein (Hoc). In this study, we describe a near-atomic structural model of Hoc by combining cryo-electron microscopy and AlphaFold structure predictions. It consists of a conserved C-terminal capsid-binding domain attached to a string of three variable immunoglobulin (Ig)-like domains, an architecture well-preserved in hundreds of Hoc molecules found in phage genomes. Each T4-Hoc fiber attaches randomly to the center of gp23* hexameric capsomers in one of the six possible orientations, though at the vertex-proximal hexamers that deviate from 6-fold symmetry, Hoc binds in two preferred orientations related by 180° rotation. Remarkably, each Hoc fiber binds to all six subunits of the capsomer, though the interactions are greatest with three of the subunits, resulting in the off-centered attachment of the C-domain. Biochemical analyses suggest that the acidic Hoc fiber (pI, ~4–5) allows for the clustering of virions in acidic pH and dispersion in neutral/alkaline pH. Hoc appears to have evolved as a sensing device that allows the phage to navigate its movements through reversible clustering–dispersion transitions so that it reaches its destination, the host bacterium, and persists in various ecological niches such as the human/mammalian gut. MDPI 2023-07-07 /pmc/articles/PMC10385173/ /pubmed/37515203 http://dx.doi.org/10.3390/v15071517 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Fokine, Andrei Islam, Mohammad Zahidul Fang, Qianglin Chen, Zhenguo Sun, Lei Rao, Venigalla B. Structure and Function of Hoc—A Novel Environment Sensing Device Encoded by T4 and Other Bacteriophages |
title | Structure and Function of Hoc—A Novel Environment Sensing Device Encoded by T4 and Other Bacteriophages |
title_full | Structure and Function of Hoc—A Novel Environment Sensing Device Encoded by T4 and Other Bacteriophages |
title_fullStr | Structure and Function of Hoc—A Novel Environment Sensing Device Encoded by T4 and Other Bacteriophages |
title_full_unstemmed | Structure and Function of Hoc—A Novel Environment Sensing Device Encoded by T4 and Other Bacteriophages |
title_short | Structure and Function of Hoc—A Novel Environment Sensing Device Encoded by T4 and Other Bacteriophages |
title_sort | structure and function of hoc—a novel environment sensing device encoded by t4 and other bacteriophages |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10385173/ https://www.ncbi.nlm.nih.gov/pubmed/37515203 http://dx.doi.org/10.3390/v15071517 |
work_keys_str_mv | AT fokineandrei structureandfunctionofhocanovelenvironmentsensingdeviceencodedbyt4andotherbacteriophages AT islammohammadzahidul structureandfunctionofhocanovelenvironmentsensingdeviceencodedbyt4andotherbacteriophages AT fangqianglin structureandfunctionofhocanovelenvironmentsensingdeviceencodedbyt4andotherbacteriophages AT chenzhenguo structureandfunctionofhocanovelenvironmentsensingdeviceencodedbyt4andotherbacteriophages AT sunlei structureandfunctionofhocanovelenvironmentsensingdeviceencodedbyt4andotherbacteriophages AT raovenigallab structureandfunctionofhocanovelenvironmentsensingdeviceencodedbyt4andotherbacteriophages |