Dual function of a highly conserved bacteriophage tail completion protein essential for bacteriophage infectivity

Autor: Isabelle Auzat, Malika Ouldali, Eric Jacquet, Beatrix Fauler, Thorsten Mielke, Paulo Tavares

Publikováno v: Communications Biology, Vol 7, Iss 1, Pp 1-12 (2024)

Abstract Infection of bacteria by phages is a complex multi-step process that includes specific recognition of the host cell, creation of a temporary breach in the host envelope, and ejection of viral DNA into the bacterial cytoplasm. These steps mus

Externí odkaz: https://doaj.org/article/69af5e1db87f433387ee5adff0114f26

The Revisited Genome of Bacillus subtilis Bacteriophage SPP1

Autor: Leonor Oliveira, Lia M. Godinho, Lina Jakutyte, Paulo Tavares, Mehdi El Sadek Fadel, Rut Carballido-López, Céline Monniot, Silvia Ayora, Isabelle Auzat, Audrey Labarde, Karima Djacem

Publikováno v: Viruses
Viruses, MDPI, 2018, 10 (12), pp.705. ⟨10.3390/v10120705⟩
Viruses 12 (10), 705. (2018)
Volume 10
Issue 12
Viruses, 2018, 10 (12), pp.705. ⟨10.3390/v10120705⟩
Digital.CSIC. Repositorio Institucional del CSIC
instname
Viruses, Vol 10, Iss 12, p 705 (2018)

Bacillus subtilis bacteriophage SPP1 is a lytic siphovirus first described 50 years ago. Its complete DNA sequence was reported in 1997. Here we present an updated annotation of the 44,016 bp SPP1 genome and its correlation to different steps of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b94eedb60355ac39edeb151511ea7cde
https://hal.archives-ouvertes.fr/hal-02178891

Role of bacteriophage SPP1 tail spike protein gp21 on host cell receptor binding and trigger of phage DNA ejection

Autor: Mário A. Santos, Catarina Baptista, Rudi Lurz, Paulo Tavares, Inês Vinga, Isabelle Auzat, Isabelle Petipas, Carlos São-José

Publikováno v: Molecular Microbiology. 83:289-303

Bacteriophages recognize and bind specific receptors to infect suitable hosts. Bacteriophage SPP1 targets at least two receptors of the Bacillus subtilis cell envelope, the glucosylated wall teichoic acids and the membrane protein YueB. Here, we iden

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::747d66f8d868243e7a23fea1e91cb8ce
https://doi.org/10.1111/j.1365-2958.2011.07931.x

Crystal Structure of Bacteriophage SPP1 Distal Tail Protein (gp19.1)

Autor: Patrick Bron, Isabelle Auzat, Christian Cambillau, Gautier Robin, Valérie Campanacci, Julie Lichière, David Veesler, Paulo Tavares

Publikováno v: Journal of Biological Chemistry. 285:36666-36673

Siphophage SPP1 infects the Gram-positive bacterium Bacillus subtilis using its long non-contractile tail and tail-tip. Electron microscopy (EM) previously allowed a low resolution assignment of most orf products belonging to these regions. We report

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8ac620ff2cc6cbe32f7750b09a130977
https://doi.org/10.1074/jbc.m110.157529

A touch of glue to complete bacteriophage assembly: the tail-to-head joining protein (THJP) family

Autor: Isabelle, Auzat, Isabelle, Petitpas, Rudi, Lurz, Frank, Weise, Paulo, Tavares

Publikováno v: Molecular microbiology. 91(6)

Bacteriophage SPP1 is a nanomachine built to infect the bacterium Bacillus subtilis. The phage particle is composed of an icosahedric capsid, which contains the viral DNA, and a long non-contractile tail. Capsids and tails are produced in infected ce

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6a8034c6ac2326658a0bcd5a98321d4a
https://pubmed.ncbi.nlm.nih.gov/24443902