Exploring Structural Diversity among Adhesion Devices Encoded by Lactococcal P335 Phages with AlphaFold2
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...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-11-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/10/11/2278 |
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| author | Adeline Goulet Jennifer Mahony Christian Cambillau Douwe van Sinderen |
| author_facet | Adeline Goulet Jennifer Mahony Christian Cambillau Douwe van Sinderen |
| author_sort | Adeline Goulet |
| collection | DOAJ |
| description | 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 <i>Lactococcus</i> 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 <i>Skunavirus</i> 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. |
| first_indexed | 2024-03-09T18:07:53Z |
| format | Article |
| id | doaj.art-5bd402357b5443c5a85a57b072b550d1 |
| institution | Directory Open Access Journal |
| issn | 2076-2607 |
| language | English |
| last_indexed | 2024-03-09T18:07:53Z |
| publishDate | 2022-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Microorganisms |
| spelling | doaj.art-5bd402357b5443c5a85a57b072b550d12023-11-24T09:17:43ZengMDPI AGMicroorganisms2076-26072022-11-011011227810.3390/microorganisms10112278Exploring Structural Diversity among Adhesion Devices Encoded by Lactococcal P335 Phages with AlphaFold2Adeline Goulet0Jennifer Mahony1Christian Cambillau2Douwe van Sinderen3Laboratoire d’Ingénierie des Systèmes Macromoléculaires (LISM), Institut de Microbiologie, Bioénergies et Biotechnologie (IM2B), Aix-Marseille Université—CNRS, UMR 7255, 13288 Marseille, FranceSchool of Microbiology, University College Cork, T12 YN60 Cork, IrelandSchool of Microbiology, University College Cork, T12 YN60 Cork, IrelandSchool of Microbiology, University College Cork, T12 YN60 Cork, IrelandBacteriophages, 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 <i>Lactococcus</i> 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 <i>Skunavirus</i> 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.https://www.mdpi.com/2076-2607/10/11/2278Bacteriophageslactococcal P335 phagesphages adhesion devicephages structurealphafold2 |
| spellingShingle | Adeline Goulet Jennifer Mahony Christian Cambillau Douwe van Sinderen Exploring Structural Diversity among Adhesion Devices Encoded by Lactococcal P335 Phages with AlphaFold2 Microorganisms Bacteriophages lactococcal P335 phages phages adhesion device phages structure alphafold2 |
| title | Exploring Structural Diversity among Adhesion Devices Encoded by Lactococcal P335 Phages with AlphaFold2 |
| title_full | Exploring Structural Diversity among Adhesion Devices Encoded by Lactococcal P335 Phages with AlphaFold2 |
| title_fullStr | Exploring Structural Diversity among Adhesion Devices Encoded by Lactococcal P335 Phages with AlphaFold2 |
| title_full_unstemmed | Exploring Structural Diversity among Adhesion Devices Encoded by Lactococcal P335 Phages with AlphaFold2 |
| title_short | Exploring Structural Diversity among Adhesion Devices Encoded by Lactococcal P335 Phages with AlphaFold2 |
| title_sort | exploring structural diversity among adhesion devices encoded by lactococcal p335 phages with alphafold2 |
| topic | Bacteriophages lactococcal P335 phages phages adhesion device phages structure alphafold2 |
| url | https://www.mdpi.com/2076-2607/10/11/2278 |
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