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Bacterial Infections

Genetic and Biochemical Analysis of Mutacin 1140, a Lantibiotic from Streptococcus mutans

J. D. Hillman, Jan Novák, Edy Sagura, Juan A. Gutierrez, T. A. Brooks, Paula J. Crowley, M. Hess, Abdul Azizi, K.-P. Leung, Dennis Cvitkovitch, A. S. Bleiweis
J. D. Hillman
Department of Oral Biology, University of Florida College of Dentistry, and
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Jan Novák
Departments of Microbiology and Oral Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294
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Edy Sagura
Interdisciplinary Center for Biological Research Protein Chemistry Core, University of Florida College of Medicine, Gainesville, Florida 32610, and
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Juan A. Gutierrez
Department of Oral Biology, University of Florida College of Dentistry, and
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T. A. Brooks
Department of Oral Biology, University of Florida College of Dentistry, and
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Paula J. Crowley
Department of Oral Biology, University of Florida College of Dentistry, and
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M. Hess
Department of Oral Biology, University of Florida College of Dentistry, and
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Abdul Azizi
Department of Oral Biology, University of Florida College of Dentistry, and
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K.-P. Leung
Department of Oral Biology, University of Florida College of Dentistry, and
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Dennis Cvitkovitch
Department of Oral Biology, University of Florida College of Dentistry, and
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A. S. Bleiweis
Department of Oral Biology, University of Florida College of Dentistry, and
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DOI: 10.1128/IAI.66.6.2743-2749.1998
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ABSTRACT

Streptococcus mutans JH1000 and its derivatives were previously shown (J. D. Hillman, K. P. Johnson, and B. I. Yaphe, Infect. Immun. 44:141–144, 1984) to produce a low-molecular-weight, broad-spectrum bacteriocin-like inhibitory substance (BLIS). The thermosensitive vector pTV1-OK harboring Tn917 was used to isolate a BLIS-deficient mutant, DM25, and the mutated gene was recovered by shotgun cloning inEscherichia coli. Sequence analysis of insert DNA adjacent to Tn917 led to the identification of four open reading frames including two (lanA and lanB) which have substantial homology to the Staphylococcus epidermidisstructural gene (epiA) and a modifying enzyme gene (epiB) for biosynthesis of the lantibiotic epidermin, respectively. Although the BLIS activity could not be recovered from broth cultures, high yields were obtained from a solid medium consisting of Todd-Hewitt broth containing 0.5% agarose that was stab inoculated with JH1140 (a spontaneous mutant of JH1000 that produces threefold-elevated amounts of activity). Agar could not substitute for agarose. Chloroform extraction of the spent medium produced a fraction which yielded two major bands on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The faster-migrating band was absent in chloroform extracts of the mutant, DM25. The amino acid sequence of this band was determined by Edman sequencing and mass spectroscopy. The results showed that it is a lantibiotic, which we have named mutacin 1140, and that the sequence corresponded to that deduced from thelanA sequence. We observed a number of similarities of mutacin 1140 to epidermin and an S. mutans lantibiotic, B-Ny266, but it appears to have significant differences in the positions of its thioether bridges. It also has other unique features with regard to its leader sequence and posttranslational modification. A proposed structure for mutacin 1140 is presented.

  • Copyright © 1998 American Society for Microbiology
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Genetic and Biochemical Analysis of Mutacin 1140, a Lantibiotic from Streptococcus mutans
J. D. Hillman, Jan Novák, Edy Sagura, Juan A. Gutierrez, T. A. Brooks, Paula J. Crowley, M. Hess, Abdul Azizi, K.-P. Leung, Dennis Cvitkovitch, A. S. Bleiweis
Infection and Immunity Jun 1998, 66 (6) 2743-2749; DOI: 10.1128/IAI.66.6.2743-2749.1998

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Genetic and Biochemical Analysis of Mutacin 1140, a Lantibiotic from Streptococcus mutans
J. D. Hillman, Jan Novák, Edy Sagura, Juan A. Gutierrez, T. A. Brooks, Paula J. Crowley, M. Hess, Abdul Azizi, K.-P. Leung, Dennis Cvitkovitch, A. S. Bleiweis
Infection and Immunity Jun 1998, 66 (6) 2743-2749; DOI: 10.1128/IAI.66.6.2743-2749.1998
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KEYWORDS

Anti-Bacterial Agents
Bacteriocins
Peptides
Streptococcus mutans

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