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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 been isolated from two STEC strains (A. D. O'Brien, J. W. Newlands, S. F. Miller, R. K. Holmes, H. W. Smith, and S. B. Formal, Science 226:694-696, 1984). In this study, we isolated two Stx2-converting phages, designated Stx2Phi -I and Stx2Phi -II, from two clinical strains of STEC associated with the outbreaks in Japan in 1996 and found that Stx2Phi -I resembled 933W, the previously reported Stx2-converting phage, in its infective properties for E. coli K-12 strain C600 while Stx2Phi -II was distinct from them. The sizes of the plaques of Stx2Phi -I and Stx2Phi -II in C600 were different; the former was larger than the latter. The restriction maps of Stx2Phi -I and Stx2Phi -II were not identical; rather, Stx2Phi -II DNA was approximately 3 kb larger than Stx2Phi -I DNA. Furthermore, Stx2Phi -I and Stx2Phi -II showed different phage immunity, with Stx2Phi -I and 933W belonging to the same group. Infection of C600 by Stx2Phi -I or 933W was affected by environmental osmolarity differently from that by Stx2Phi -II. When C600 was grown under conditions of high osmolarity, the infectivity of Stx2Phi -I and 933W was greatly decreased compared with that of Stx2Phi -II. Examination of the plating efficiency of the three phages for the defined mutations in C600 revealed that the efficiency of Stx2Phi -I and 933W for the fadL mutant decreased to less than 10-7 compared with that for C600 whereas the efficiency of Stx2Phi -II decreased to 0.1% of that for C600. In contrast, while the plating efficiency of Stx2Phi -II for the lamB mutant decreased to a low level (0.05% of that for C600), the efficiencies of Stx2Phi -I and 933W were not changed. This was confirmed by the phage neutralization experiments with isolated outer membrane fractions from C600, fadL mutant, or lamB mutant or the purified His6-tagged FadL and LamB proteins. Based on the data, we concluded that FadL acts as the receptor for Stx2Phi -I and Stx2Phi -II whereas LamB acts as the receptor only for Stx2Phi -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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