Characterization of Mu-Like
            <i>Yersinia</i>
            Phages Exhibiting Temperature Dependent Infection

Meng, Biao; Qi, Zhizhen; Li, Xiang; Peng, Hong; Bi, Shanzheng; Wei, Xiao; Li, Yan; Zhang, Qi; Xu, Xiaoqing; Zhao, Haihong; Yang, Xiaoyan; Wang, Changjun; Zhao, Xiangna

doi:10.1128/spectrum.00203-23

Microbiol Spectr

2023

DOI: 10.1128/spectrum.00203-23

|View full text |Cite

Characterization of Mu-Like Yersinia Phages Exhibiting Temperature Dependent Infection

Biao Meng,

Zhizhen Qi,

Xiang Li

et al.

Abstract: Mu-like bacteriophages of Y. pestis were isolated from M. himalayana of the Qinghai-Tibetan plateau in China. These bacteriophages have a unique temperature dependent life cycle, follow a lytic cycle at the temperature of warm-blooded mammals (37°С), and enter the lysogenic cycle at the temperature of its flea-vector (26°С).

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2024

Publication Types

Select...

Article2

Relationship

Self Cite0

Independent2

Authors

Journals

Cited by 2 publications

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Insights into the genomic traits of Yersinia frederiksenii, Yersinia intermedia and Yersinia kristensenii isolated from diverse sources in Brazil

Vilela,

Imori,

Allard

et al. 2024

Antonie van Leeuwenhoek

View full text Add to dashboard Cite

Insights into the genomic traits of Yersinia frederiksenii, Yersinia intermedia and Yersinia kristensenii isolated from diverse sources in Brazil

Vilela,

Imori,

Allard

et al. 2024

Antonie van Leeuwenhoek

View full text Add to dashboard Cite

The tal gene of lactococcal bacteriophage TP901-1 is involved in DNA release following host adsorption

Ruiz-Cruz,

Erazo Garzon,

Cambillau

et al. 2024

Appl Environ Microbiol

View full text Add to dashboard Cite

Temperate P335 phage TP901-1 represents one of the best-characterized Gram-positive phages regarding its structure and host interactions. Following its reversible adsorption to the polysaccharidic side-chain of the cell wall polysaccharide of its host Lactococcus cremoris 3107, TP901-1 requires a glucosylated cell envelope moiety to trigger its genome delivery into the host cytoplasm. Here, we demonstrate that three distinct single amino acid substitutions in the Tal protein of TP901-1 baseplate are sufficient to overcome the TP901-1 resistance of three L. cremoris 3107 derivatives, whose resistance is due to impaired DNA release of the phage. All of these Tal alterations are located in the N-terminally located gp27-like domain of the protein, conserved in many tailed phages. AlphaFold2 predictions of the Tal mutant proteins suggest that these mutations favor conformational changes necessary to reposition the Tal fiber and thus facilitate release of the tape measure protein from the tail tube and subsequent DNA ejection in the absence of the trigger otherwise required for phage genome release. IMPORTANCE Understanding the molecular mechanisms involved in phage-host interactions is essential to develop phage-based applications in the food and probiotic industries, yet also to reduce the risk of phage infections in fermentations. Lactococcus , extensively used in dairy fermentations, has been widely employed to unravel such interactions. Phage infection commences with the recognition of a suitable host followed by the release of its DNA into the bacterial cytoplasm. Details on this latter, irreversible step are still very scarce in lactococci and other Gram-positive bacteria. We demonstrate that a component of the baseplate of the lactococcal phage TP901-1, the tail-associated lysin (Tal), is involved in the DNA delivery into its host, L. cremoris 3107. Specifically, we have found that three amino acid changes in Tal appear to facilitate structural rearrangements in the baseplate necessary for the DNA release process, even in the absence of an otherwise required host trigger.

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Characterization of Mu-Like Yersinia Phages Exhibiting Temperature Dependent Infection

Cited by 2 publications

References 40 publications

Insights into the genomic traits of Yersinia frederiksenii, Yersinia intermedia and Yersinia kristensenii isolated from diverse sources in Brazil

Insights into the genomic traits of Yersinia frederiksenii, Yersinia intermedia and Yersinia kristensenii isolated from diverse sources in Brazil

The tal gene of lactococcal bacteriophage TP901-1 is involved in DNA release following host adsorption

Contact Info

Product

Resources

About