Crystal Structure of the Receptor-Binding Protein Head Domain from Lactococcus lactis Phage bIL170-Reference-Cited by-同舟云学术

Crystal Structure of the Receptor-Binding Protein Head Domain from Lactococcus lactis Phage bIL170

Published:2006-09-15 Issue:18 Volume:80 Page:9331-9335
ISSN:0022-538X
Container-title:Journal of Virology
language:en
Short-container-title:J Virol

Author:

Ricagno Stefano¹,Campanacci Valérie¹,Blangy Stéphanie¹,Spinelli Silvia¹,Tremblay Denise²³,Moineau Sylvain²³⁴,Tegoni Mariella¹,Cambillau Christian¹

Affiliation:

1. Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités Aix-Marseille I & II, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France

2. Groupe de Recherche en Écologie Buccale (GREB), Faculté de Médecine Dentaire

3. Félix d'Hérelle Reference Center for Bacterial Viruses

4. Département de Biochimie et de Microbiologie, Faculté des Sciences et de Génie, Université Laval, Québec City, Québec, Canada G1K 7P4

Abstract

ABSTRACT Lactococcus lactis , a gram-positive bacterium widely used by the dairy industry, is subject to lytic phage infections. In the first step of infection, phages recognize the host saccharidic receptor using their receptor binding protein (RBP). Here, we report the 2.30-Å-resolution crystal structure of the RBP head domain from phage bIL170. The structure of the head monomer is remarkably close to those of other lactococcal phages, p2 and TP901-1, despite any sequence identity with them. The knowledge of the three-dimensional structures of three RBPs gives a better insight into the module exchanges which have occurred among phages.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JVI.01160-06

Reference25 articles.

1. Bourne, Y., J. Mazurier, D. Legrand, P. Rouge, J. Montreuil, G. Spik, and C. Cambillau. 1994. Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety. Structure2:209-219.

2. Bourne, Y., A. Roussel, M. Frey, P. Rouge, J. C. Fontecilla-Camps, and C. Cambillau. 1990. Three-dimensional structures of complexes of Lathyrus ochrus isolectin I with glucose and mannose: fine specificity of the monosaccharide-binding site. Proteins8:365-376.

3. The CCP4 suite: programs for protein crystallography

4. Crutz-Le Coq, A. M., B. Cesselin, J. Commissaire, and J. Anba. 2002. Sequence analysis of the lactococcal bacteriophage bIL170: insights into structural proteins and HNH endonucleases in dairy phages. Microbiology148:985-1001.

5. Llama Antibodies against a Lactococcal Protein Located at the Tip of the Phage Tail Prevent Phage Infection

Cited by 62 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

2. A host recognition module shared among distantAlteromonasbacteriophage families features tail fibers with transient chaperone “caps”;2023-03-07

3. Exploring Structural Diversity among Adhesion Devices Encoded by Lactococcal P335 Phages with AlphaFold2;Microorganisms;2022-11-16

4. Potential of bacteriophage proteins as recognition molecules for pathogen detection;Critical Reviews in Biotechnology;2022-07-18

5. Structure and Topology Prediction of Phage Adhesion Devices Using AlphaFold2: The Case of Two Oenococcus oeni Phages;Microorganisms;2021-10-14