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Journal of Bacteriology, May 2002, p. 2455-2459, Vol. 184, No. 9
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.9.2455-2459.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

A Conserved C-Terminal Region in Gp71 of the Small Isometric-Head Phage LL-H and ORF474 of the Prolate-Head Phage JCL1032 Is Implicated in Specificity of Adsorption of Phage to Its Host, Lactobacillus delbrueckii

Department of Biology, University of Oulu, FIN-90014 Oulu,¹ Biotechnology Laboratory, REDEC of Kajaani, University of Oulu, FIN-88600 Sotkamo, Finland²

Received 22 January 2001/ Accepted 5 February 2002

Thirty-five phage-resistant mutants of Lactobacillus delbrueckii subsp. lactis ATCC 15808 were selected. Thirty-three of these mutants were assigned to the Bes group, while the remaining two were grouped under the Ads designation. Bes group mutants adsorbed phage LL-H but did not allow efficient phage development. Preliminary evidence suggests that these strains exhibit a mutation that changes the DNA specificity of a restriction-modification system. The Ads group mutants did not adsorb the small isometric-head phage LL-H. The results suggest that there are at least three different types of phage receptors in L. delbrueckii: two that are specific for small isometric-head phages and one that is specific for prolate-head phage JCL1032. Five LL-H host-range mutants which could overcome the adsorption block (a-type mutants) were selected and investigated by sequencing the genes g71 and g17, which encode minor and major tail proteins, respectively. Each of the a-type mutants carried a nucleotide change at the 3' end of gene g71. No mutations were observed in gene g17. Comparison of the gene product of g71 of phage LL-H with its homolog in JCL1032 (ORF474) showed that these proteins had very similar C-terminal regions. No similarities were found at the N-terminal part of the proteins. We conclude that the C-terminal portion of the protein encoded by g71 of phage LL-H and its homolog in phage JCL1032 determines the adsorption specificities of these phages on L. delbrueckii.

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