Exploring structural diversity among adhesion devices encoded by lactococcal P335 phages with AlphaFold2
| dc.contributor.author | Goulet, Adeline | en |
| dc.contributor.author | Mahony, Jennifer | en |
| dc.contributor.author | Cambillau, Christian | en |
| dc.contributor.author | van Sinderen, Douwe | en |
| dc.contributor.funder | Science Foundation Ireland | |
| dc.date.accessioned | 2023-05-10T12:06:00Z | |
| dc.date.available | 2023-05-10T12:41:55Z | en |
| dc.date.available | 2023-05-10T12:06:00Z | |
| dc.date.issued | 2022-11 | en |
| dc.date.updated | 2023-05-10T11:41:58Z | en |
| dc.description.abstract | Bacteriophages, or phages, are the most abundant biological entities on Earth. They possess molecular nanodevices to package and store their genome, as well as to introduce it into the cytoplasm of their bacterial prey. Successful phage infection commences with specific recognition of, and adhesion to, a suitable host cell surface. Adhesion devices of siphophages infecting Gram-positive bacteria are very diverse and remain, for the majority, poorly understood. These assemblies often comprise long, flexible, and multi-domain proteins, which limit their structural analyses by experimental approaches. The protein structure prediction program AlphaFold2 is exquisitely adapted to unveil structural and functional details of such molecular machineries. Here, we present structure predictions of adhesion devices from siphophages belonging to the P335 group infecting Lactococcus spp., one of the most extensively applied lactic acid bacteria in dairy fermentations. The predictions of representative adhesion devices from types I-IV P335 phages illustrate their very diverse topology. Adhesion devices from types III and IV phages share a common topology with that of Skunavirus p2, with a receptor binding protein anchored to the virion by a distal tail protein loop. This suggests that they exhibit an activation mechanism similar to that of phage p2 prior to host binding. | en |
| dc.description.status | Peer reviewed | en |
| dc.format.mimetype | application/pdf | en |
| dc.identifier.articleid | 2278 | |
| dc.identifier.citation | Goulet, A., Mahony, J., Cambillau, C. and Van Sinderen, D. (2022) ‘Exploring structural diversity among adhesion devices encoded by lactococcal P335 phages with AlphaFold2’, Microorganisms, 10 (11), 2278. doi: 10.3390/microorganisms10112278 | |
| dc.identifier.doi | 10.3390/microorganisms10112278 | en |
| dc.identifier.eissn | 2076-2607 | |
| dc.identifier.endpage | 14 | |
| dc.identifier.issued | 11 | |
| dc.identifier.journaltitle | Microorganisms | |
| dc.identifier.startpage | 1 | |
| dc.identifier.uri | https://hdl.handle.net/10468/14448 | |
| dc.identifier.volume | 10 | |
| dc.language.iso | en | en |
| dc.publisher | MDPI | |
| dc.relation.project | info:eu-repo/grantAgreement/SFI/SFI Research Centres/12/RC/2273/IE/Alimentary Pharmabiotic Centre (APC) - Interfacing Food & Medicine/ | |
| dc.relation.project | info:eu-repo/grantAgreement/SFI/SFI Frontiers for the Future::Project/20/FFP-P/8664/IE/The sweet tooth of a bacterial virus: Unravelling Phage-Host Attachment and Recognition Modalities (PHARM) in the dairy bacterium Streptococcus thermophilus/ | |
| dc.rights | © 2022 by the authors. 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/). | |
| dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
| dc.subject | Bacteriophages | |
| dc.subject | Lactococcal P335 phages | |
| dc.subject | Phages adhesion device | |
| dc.subject | Phages structure | |
| dc.subject | Alphafold2 | |
| dc.title | Exploring structural diversity among adhesion devices encoded by lactococcal P335 phages with AlphaFold2 | en |
| dc.type | Article (peer-reviewed) |
