Zhiying Wu, Haixia Huang, Shihui Peng, Heng-Keat Tam, Ying Liu, Lili Chen, Qinqin Bai
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引用次数: 0
Abstract
PB1-like phages belong to Pbunavirus and are widespread in various environments. This group of phages is a promising candidate for treating human or animal infectious diseases caused by antibiotic-resistant P. aeruginosa. The lipopolysaccharide (LPS) has been identified as the receptor of different PB1-like phages, while little is known about the receptor-binding proteins (RBPs) of these phages. We constructed the tail fiber protein (gp50) of a PB1-like phage, PHW2, and its C- or N-terminus truncation variants to identify its role during the phage infection. The anti-gp50(453-964) antibody showed a similar effect to the antibody against gp50 in blocking the phage infection. The protein competition and cell binding assays showed that the gp50(1-451) doesn't exhibit an effect on the adsorption of the host cells. These results indicated that the C-terminus of gp50 is the essential region that mediates phage PHW2 adsorption and infection.
期刊介绍：
Viruses are convenient models for the elucidation of life processes. The study of viruses is again on the cutting edge of biological sciences: systems biology, genomics, proteomics, metagenomics, using the newest most powerful tools.
Huge amounts of new details on virus interactions with the cell, other pathogens and the hosts – animal (including human), insect, fungal, plant, bacterial, and archaeal - and their role in infection and disease are forthcoming in perplexing details requiring analysis and comments.
Virus Genes is dedicated to the publication of studies on the structure and function of viruses and their genes, the molecular and systems interactions with the host and all applications derived thereof, providing a forum for the analysis of data and discussion of its implications, and the development of new hypotheses.
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