Bacillus subtilis Operon Encoding a Membrane Receptor for Bacteriophage SPP1

Author:

São-José Carlos1,Baptista Catarina1,Santos Mário A.1

Affiliation:

1. Centro de Genética e Biologia Molecular e Departamento de Biologia Vegetal, Faculdade de Ciências da Universidade de Lisboa, Lisbon, Portugal

Abstract

ABSTRACT The results reported here have identified yueB as the essential gene involved in irreversible binding of bacteriophage SPP1 to Bacillus subtilis . First, a deletion in an SPP1-resistant ( pha-2 ) strain, covering most of the yueB gene, could be complemented by a xylose-inducible copy of yueB inserted at amyE . Second, disruption of yueB by insertion of a pMutin4 derivative resulted in a phage resistance phenotype regardless of the presence or absence of IPTG (isopropyl-β- d -thiogalactopyranoside). YueB homologues are widely distributed in gram-positive bacteria. The protein Pip, which also serves as a phage receptor in Lactococcus lactis , belongs to the same family. yueB encodes a membrane protein of ∼120 kDa, detected in immunoblots together with smaller forms that may be processed products arising from cleavage of its long extracellular domain. Insertional inactivation of yueB and the surrounding genes indicated that yueB is part of an operon which includes at least the upstream genes yukE , yukD , yukC , and yukBA . Disruption of each of the genes in the operon allowed efficient irreversible adsorption, provided that yueB expression was retained. Under these conditions, however, smaller plaques were produced, a phenotype which was particularly noticeable in yukE mutant strains. Interestingly, such reduction in plaque size was not correlated with a decreased adsorption rate. Overall, these results provide the first demonstration of a membrane-bound protein acting as a phage receptor in B. subtilis and suggest an additional involvement of the yukE operon in a step subsequent to irreversible adsorption.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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