Identification of the Lipopolysaccharide Core of Yersinia pestis and Yersinia pseudotuberculosis as the Receptor for Bacteriophage φA1122

Kiljunen, Saija; Datta, Neeta; Dentovskaya, Svetlana V.; Anisimov, Andrey P.; Knirel, Yuriy A.; Bengoechea, José A.; Holst, Otto; Skurnik, Mikael

doi:10.1128/jb.00339-11

Cited by 83 publications

(91 citation statements)

References 78 publications

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“…LB was used as a non- adsorbing control in each assay, and the phage titer in the control supernatant was set to 100%. Each assay was performed in duplicate and repeated twice (15). Periodate and proteinase K treatments.…”

Section: Methodsmentioning

confidence: 99%

“…Based on the spectra of lytic activity, Yep-phi is much more specific for Y. pestis than the other diagnostic phage, PhiA1122, which is used by the Centers for Disease Control and Prevention of the United States for the identification of Y. pestis. Y. pseudotuberculosis is also infected by PhiA1122 when grown at 37°C (15). The PhiA1122 receptor is demonstrated to be the common lipopolysaccharide (LPS) core of Y. pestis and Y. pseudotuberculosis.…”

mentioning

confidence: 99%

“…The LPS of Y. pestis is O antigen deficient and restricted to the core and lipid A moieties (22). Much of the available detailed information about the receptors of Y. pestis phages focuses on the LPS (15,23). The LPS of Y. pestis has been studied extensively in terms of structure, activity, composition, modification, virulence, and assembly (15,(22)(23)(24).…”

mentioning

confidence: 99%

“…The PhiA1122 receptor is demonstrated to be the common lipopolysaccharide (LPS) core of Y. pestis and Y. pseudotuberculosis. The receptor used by phage Yep-phi for adsorption has not yet been identified (15).…”

mentioning

confidence: 99%

“…Much of the available detailed information about the receptors of Y. pestis phages focuses on the LPS (15,23). The LPS of Y. pestis has been studied extensively in terms of structure, activity, composition, modification, virulence, and assembly (15,(22)(23)(24). The receptor was identified as the LPS of Y. pestis for eight bacteriophages, including L-413C, P2 vir1, PhiJA1, PhiA1122, Pokrovskaya, T7 Yp , Y, and PST (23).…”

mentioning

confidence: 99%

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Outer Membrane Proteins Ail and OmpF of Yersinia pestis Are Involved in the Adsorption of T7-Related Bacteriophage Yep-phi

Zhao

Cui

Yan

et al. 2013

J Virol

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Yep-phi is a T7-related bacteriophage specific to Yersinia pestis, and it is routinely used in the identification of Y. pestis in China. Yep-phi infects Y. pestis grown at both 20°C and 37°C. It is inactive in other Yersinia species irrespective of the growth temperature. Based on phage adsorption, phage plaque formation, affinity chromatography, and Western blot assays, the outer membrane proteins of Y. pestis Ail and OmpF were identified to be involved, in addition to the rough lipopolysaccharide, in the adsorption of Yep-phi. The phage tail fiber protein specifically interacts with Ail and OmpF proteins, and residues 518N, 519N, and 523S of the phage tail fiber protein are essential for the interaction with OmpF, whereas residues 518N, 519N, 522C, and 523S are essential for the interaction with Ail. This is the first report to demonstrate that membrane-bound proteins are involved in the adsorption of a T7-related bacteriophage. The observations highlight the importance of the tail fiber protein in the evolution and function of various complex phage systems and provide insights into phage-bacterium interactions.

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Outer Membrane Proteins Ail and OmpF of Yersinia pestis Are Involved in the Adsorption of T7-Related Bacteriophage Yep-phi

Zhao

Cui

Yan

et al. 2013

J Virol

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Proteomic analysis and protein structure prediction of Shigella phage Sfk20 based on a comparative study using structure prediction approaches

Mallick,

Dutta,

Mondal

et al. 2023

Proteins

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Bacteriophages are the natural predators of bacteria and are available abundantly everywhere in nature. Lytic phages can specifically infect their bacterial host (through attachment to the receptor) and use their host replication machinery to replicate rapidly, a feature that enables them to kill a disease‐causing bacteria. Hence, phage attachment to the host bacteria is the first important step of the infection process. It is reported in this study that the receptor could be an LPS which is responsible for the attachment of the Sfk20 phage to its host (Shigella flexneri 2a). Phage Sfk20 bacteriolytic activity was examined for preliminary optimization of phage titer. The phage Sfk20 viability at different saline conditions was conducted. The LC–MS/MS technique used here for detecting and identifying 40 Sfk20 phage proteins helped us to get an initial understanding of the structural landscape of phage Sfk20. From the identified proteins, six structurally significant proteins were selected for structure prediction using two neural network systems: AlphaFold2 and ESMFold, and one homology modeling software: Phyre2. Later the performance of these modeling systems was compared using various metrics. We conclude from the available and generated information that AlphaFold2 and Phyre2 perform better than ESMFold for predicting Sfk20 phage protein structures.

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Yersinia Surface Structures and Bacteriophages

Skurnik

2012

Advances in Yersinia Research

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Identification of the Lipopolysaccharide Core of Yersinia pestis and Yersinia pseudotuberculosis as the Receptor for Bacteriophage φA1122

Abstract: A1122 is a T7-related bacteriophage infecting most isolates of

Cited by 83 publications

References 78 publications

Outer Membrane Proteins Ail and OmpF of Yersinia pestis Are Involved in the Adsorption of T7-Related Bacteriophage Yep-phi

Outer Membrane Proteins Ail and OmpF of Yersinia pestis Are Involved in the Adsorption of T7-Related Bacteriophage Yep-phi

Proteomic analysis and protein structure prediction of Shigella phage Sfk20 based on a comparative study using structure prediction approaches

Yersinia Surface Structures and Bacteriophages

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