Identification and Characterization of a Newly Isolated Shiga Toxin 2-Converting Phage from Shiga Toxin-Producing Escherichia coli

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Infection and Immunity, September 1998, p. 4100-4107, Vol. 66, No. 9
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Identification and Characterization of a Newly Isolated Shiga Toxin 2-Converting Phage from Shiga Toxin-Producing Escherichia coli

Masahisa Watarai,¹^,² Toshio Sato,¹ Midori Kobayashi,¹ Takeshi Shimizu,¹ Shinji Yamasaki,¹ Toru Tobe,² Chihiro Sasakawa,² and Yoshifumi Takeda¹^,^*

Research Institute, International Medical Center of Japan, Tokyo 162,¹ and Department of Bacteriology, Institute of Medical Science, University of Tokyo, Tokyo 108,² Japan

Received 20 April 1998/Returned for modification 22 May 1998/Accepted 2 June 1998

Shiga toxins 1 (Stx1) and 2 (Stx2) are encoded by toxin-converting bacteriophages of Stx-producing Escherichia coli (STEC),and so far two Stx1- and one Stx2-converting phages have beenisolated from two STEC strains (A. D. O'Brien, J. W. Newlands,S. F. Miller, R. K. Holmes, H. W. Smith, and S. B. Formal, Science226:694-696, 1984). In this study, we isolated two Stx2-convertingphages, designated Stx2 $Phi$ -I and Stx2 $Phi$ -II, from two clinical strainsof STEC associated with the outbreaks in Japan in 1996 and foundthat Stx2 $Phi$ -I resembled 933W, the previously reported Stx2-convertingphage, in its infective properties for E. coli K-12 strain C600while Stx2 $Phi$ -II was distinct from them. The sizes of the plaquesof Stx2 $Phi$ -I and Stx2 $Phi$ -II in C600 were different; the former waslarger than the latter. The restriction maps of Stx2 $Phi$ -I and Stx2 $Phi$ -IIwere not identical; rather, Stx2 $Phi$ -II DNA was approximately 3 kblarger than Stx2 $Phi$ -I DNA. Furthermore, Stx2 $Phi$ -I and Stx2 $Phi$ -II showeddifferent phage immunity, with Stx2 $Phi$ -I and 933W belonging to thesame group. Infection of C600 by Stx2 $Phi$ -I or 933W was affectedby environmental osmolarity differently from that by Stx2 $Phi$ -II.When C600 was grown under conditions of high osmolarity, the infectivityof Stx2 $Phi$ -I and 933W was greatly decreased compared with that ofStx2 $Phi$ -II. Examination of the plating efficiency of the three phagesfor the defined mutations in C600 revealed that the efficiencyof Stx2 $Phi$ -I and 933W for the fadL mutant decreased to less than10⁷ compared with that for C600 whereas the efficiency of Stx2 $Phi$ -IIdecreased to 0.1% of that for C600. In contrast, while the platingefficiency of Stx2 $Phi$ -II for the lamB mutant decreased to a lowlevel (0.05% of that for C600), the efficiencies of Stx2 $Phi$ -I and933W were not changed. This was confirmed by the phage neutralizationexperiments with isolated outer membrane fractions from C600,fadL mutant, or lamB mutant or the purified His₆-tagged FadL andLamB proteins. Based on the data, we concluded that FadL actsas the receptor for Stx2 $Phi$ -I and Stx2 $Phi$ -II whereas LamB acts asthe receptor only for Stx2 $Phi$ -II.

^* Corresponding author. Mailing address: Research Institute, International Medical Center of Japan, 1-21-1, Toyama, Shinjuku-ku,Tokyo 162, Japan. Phone: 81-3-5273-6844. Fax: 81-3-3202-7364.E-mail: resedr{at}imcj.go.jp.

Infection and Immunity, September 1998, p. 4100-4107, Vol. 66, No. 9
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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