Title Insights into the Alcyoneusvirus adsorption complex /
Authors Noreika, Algirdas ; Rutkienė, Rasa ; Dumalakienė, Irena ; Vilienė, Rita ; Laurynėnas, Audrius ; Povilonienė, Simona ; Skapas, Martynas ; Meškys, Rolandas ; Kalinienė, Laura
DOI 10.3390/ijms24119320
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Is Part of International journal of molecular sciences.. Basel : MDPI AG. 2023, vol. 24, iss. 11, art. no. 9320, p. 1-22.. ISSN 1661-6596. eISSN 1422-0067
Keywords [eng] adsorption ; Alcyoneusvirus ; Klebsiella pneumoniae phage ; tail fibers ; vB_KleM_RaK2
Abstract [eng] The structures of the Caudovirales phage tails are key factors in determining the host specificity of these viruses. However, because of the enormous structural diversity, the molecular anatomy of the host recognition apparatus has been elucidated in only a number of phages. Klebsiella viruses vB_KleM_RaK2 (RaK2) and phiK64-1, which form a new genus Alcyoneusvirus according to the ICTV, have perhaps one of the most structurally sophisticated adsorption complexes of all tailed viruses described to date. Here, to gain insight into the early steps of the alcyoneusvirus infection process, the adsorption apparatus of bacteriophage RaK2 is studied in silico and in vitro. We experimentally demonstrate that ten proteins, gp098 and gp526–gp534, previously designated as putative structural/tail fiber proteins (TFPs), are present in the adsorption complex of RaK2. We show that two of these proteins, gp098 and gp531, are essential for attaching to Klebsiella pneumoniae KV-3 cells: gp531 is an active depolymerase that recognizes and degrades the capsule of this particular host, while gp098 is a secondary receptor-binding protein that requires the coordinated action of gp531. Finally, we demonstrate that RaK2 long tail fibers consist of nine TFPs, seven of which are depolymerases, and propose a model for their assembly.
Published Basel : MDPI AG
Type Journal article
Language English
Publication date 2023
CC license CC license description