Evolved distal tail carbohydrate binding modules of L actobacillus phage J-1: a novel type of anti-receptor widespread among lactic acid bacteria phages

Autor: Dieterle, Maria-Eugenia, Spinelli, Silvia, Sadovskaya, Irina, Piuri, Mariana, Cambillau, Christian
Přispěvatelé: Architecture et fonction des macromolécules biologiques (AFMB), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Instituto de Química Biológica Ciencias Exactas y Naturales (IQUIBICEN), Consejo Nacional de Investigaciones Científicas y Técnicas [Buenos Aires] (CONICET)-Departamento de Quimica Biológica, Facultad de Ciencias Exactas y Naturales [Buenos Aires] (FCEyN), Universidad de Buenos Aires [Buenos Aires] (UBA)-Universidad de Buenos Aires [Buenos Aires] (UBA)-Facultad de Ciencias Exactas y Naturales [Buenos Aires] (FCEyN), Universidad de Buenos Aires [Buenos Aires] (UBA)-Universidad de Buenos Aires [Buenos Aires] (UBA), LR2B UMT 08, Bassin Napoleon, Univ Littoral Cote dOpale, Université du Littoral Côte d'Opale (ULCO), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Departamento de Quimica Biológica, Universidad de Buenos Aires [Buenos Aires] (UBA)-Universidad de Buenos Aires [Buenos Aires] (UBA)-Consejo Nacional de Investigaciones Científicas y Técnicas [Buenos Aires] (CONICET)
Jazyk: angličtina
Rok vydání: 2017
Předmět:
[SDV.BIO]Life Sciences [q-bio]/Biotechnology
MESH: Host Specificity
Protein Conformation
[SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology
Carbohydrates
MESH: Microscopy
Electron
[SDV.IMM.II]Life Sciences [q-bio]/Immunology/Innate immunity
Host Specificity
Structure-Activity Relationship
MESH: Protein Conformation
MESH: Structure-Activity Relationship
[SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases
MESH: Protein Binding
Bacteriophages
Lactic Acid
MESH: Bacteriophages
MESH: Viral Tail Proteins
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biochemistry [q-bio.BM]
[SDV.MHEP.ME]Life Sciences [q-bio]/Human health and pathology/Emerging diseases
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
MESH: Lactobacillus casei
Virion
Viral Tail Proteins
[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]
[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biomolecules [q-bio.BM]
Lactococcus lactis
Lactobacillus
Lacticaseibacillus casei
Microscopy
Electron
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biomolecules [q-bio.BM]
MESH: Lactococcus lactis
[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology
[SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology
MESH: Virion
MESH: Lactic Acid
MESH: Lactobacillus
Protein Binding
MESH: Carbohydrates
Zdroj: Molecular Microbiology
Molecular Microbiology, Wiley, 2017, 104 (4), pp.608-620. ⟨10.1111/mmi.13649⟩
Molecular Microbiology, 2017, 104 (4), pp.608-620. ⟨10.1111/mmi.13649⟩
ISSN: 0950-382X
1365-2958
DOI: 10.1111/mmi.13649⟩
Popis: International audience; Bacteriophage replication requires specific host-recognition. Some siphophages harbour a large complex, the baseplate, at the tip of their non-contractile tail. This baseplate holds receptor binding proteins (RBPs) that can recognize the host cell-wall polysaccharide (CWPS) and specifically attach the phage to its host. While most phages possess a dedicated RBP, the phage J-1 that infects Lactobacillus casei seemed to lack one. It has been shown that the phage J-1 distal tail protein (Dit) plays a role in host recognition and that its sequence comprises two inserted modules compared with 'classical' Dits. The first insertion is similar to carbohydrate-binding modules (CBMs), whereas the second insertion remains undocumented. Here, we determined the structure of the second insertion and found it also similar to several CBMs. Expressed insertion CBM2, but not CBM1, binds to L. casei cells and neutralize phage attachment to the bacterial cell wall and the isolated and purified CWPS of L. casei BL23 prevents CBM2 attachment to the host. Electron microscopy single particle reconstruction of the J-1 virion baseplate revealed that CBM2 is projected at the periphery of Dit to optimally bind the CWPS receptor. Taken together, these results identify J-1 evolved Dit as the phage RBP.
Databáze: OpenAIRE
Externí odkaz: