This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bormann, C.
Right arrow Articles by Schwarz, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bormann, C.
Right arrow Articles by Schwarz, H.

 Previous Article  |  Next Article 

Journal of Bacteriology, December 1999, p. 7421-7429, Vol. 181, No. 24
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Characterization of a Novel, Antifungal, Chitin-Binding Protein from Streptomyces tendae Tü901 That Interferes with Growth Polarity

Christiane Bormann,1,* Daniel Baier,1 Ingmar Hörr,2 Claudia Raps,1 Jürgen Berger,3 Günther Jung,2 and Heinz Schwarz3

Mikrobiologie/Biotechnologie1 and Organische Chemie,2 Universität Tübingen, and Max-Planck-Institut für Entwicklungsbiologie,3 D-72076 Tübingen, Germany

Received 3 August 1999/Accepted 27 September 1999

The afp1 gene, which encodes the antifungal protein AFP1, was cloned from nikkomycin-producing Streptomyces tendae Tü901, using a nikkomycin-negative mutant as a host and screening transformants for antifungal activity against Paecilomyces variotii in agar diffusion assays. The 384-bp afp1 gene has a low G+C content (63%) and a transcription termination structure with a poly(T) region, unusual attributes for Streptomyces genes. AFP1 was purified from culture filtrate of S. tendae carrying the afp1 gene on the multicopy plasmid pIJ699. The purified protein had a molecular mass of 9,862 Da and lacked a 42-residue N-terminal peptide deduced from the nucleotide sequence. AFP1 was stable at extreme pH values and high temperatures and toward commercial proteinases. AFP1 had limited similarity to cellulose-binding domains of microbial plant cell wall hydrolases and bound to crab shell chitin, chitosan, and cell walls of P. variotii but showed no enzyme activity. The biological activity of AFP1, which represents the first chitin-binding protein from bacteria exhibiting antifungal activity, was directed against specific ascomycetes, and synergistic interaction with the chitin synthetase inhibitor nikkomycin inhibited growth of Aspergillus species. Microscopy studies revealed that fluorescein-labeled AFP1 strongly bound to the surface of germinated conidia and to tips of growing hyphae, causing severe alterations in cell morphogenesis that gave rise to large spherical conidia and/or swollen hyphae and to atypical branching.

* Corresponding author. Mailing address: Mikrobiologie/Biotechnologie, Universität Tübingen, Auf der Morgenstelle 15, D-72076 Tübingen, Germany. Phone: (49) 7071 297 7620. Fax: (49) 7071 29 4634. E-mail: christiane.bormann{at}uni-tuebingen.de.

Journal of Bacteriology, December 1999, p. 7421-7429, Vol. 181, No. 24
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Hissa, D. C., Vasconcelos, I. M., Carvalho, A. F. U., Nogueira, V. L. R., Cascon, P., Antunes, A. S. L., de Macedo, G. R., Melo, V. M. M. (2008). Novel surfactant proteins are involved in the structure and stability of foam nests from the frog Leptodactylus vastus. J. Exp. Biol. 211: 2707-2711 [Abstract] [Full Text]  
  • Theis, T., Wedde, M., Meyer, V., Stahl, U. (2003). The Antifungal Protein from Aspergillus giganteus Causes Membrane Permeabilization. Antimicrob. Agents Chemother. 47: 588-593 [Abstract] [Full Text]  
  • Selitrennikoff, C. P. (2001). Antifungal Proteins. Appl. Environ. Microbiol. 67: 2883-2894 [Full Text]  
  • Chu, H. H., Hoang, V., Hofemeister, J., Schrempf, H. (2001). A Bacillus amyloliquefaciens ChbB protein binds {beta}- and {{alpha}}-chitin and has homologues in related strains. Microbiology 147: 1793-1803 [Abstract] [Full Text]  
  • Saito, A., Miyashita, K., Schrempf, H. (2001). Characteristics of a Streptomyces coelicolor A3(2) Extracellular Protein Targeting Chitin and Chitosan. Appl. Environ. Microbiol. 67: 1268-1273 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»