Literature DB >> 19431044

Immunoaffinity purification of the class V chitin synthase of Wangiella (Exophiala) dermatitidis.

Dariusz Abramczyk1, Paul J Szaniszlo.   

Abstract

The class V chitin synthase is unique because it has a myosin motor-like domain fused to its catalytic domain. The biochemical properties of this enzyme and its function remain undefined beyond the knowledge that it is the only single chitin synthase required for sustained cell growth at elevated temperatures and, consequently, virulence. This report describes our successful efforts to isolate and purify an active and soluble form of the enzyme from the cell membranes of Wangiella by using a specific polyclonal antibody. To our knowledge, this is the first purification of a single chitin synthase of a filamentous fungus.

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Year:  2009        PMID: 19431044      PMCID: PMC2727359          DOI: 10.1080/10826060902953244

Source DB:  PubMed          Journal:  Prep Biochem Biotechnol        ISSN: 1082-6068            Impact factor:   2.162


  16 in total

Review 1.  Chitin synthesis in human pathogenic fungi.

Authors:  C A Munro; N A Gow
Journal:  Med Mycol       Date:  2001       Impact factor: 4.076

Review 2.  Evolution and phylogenetic relationships of chitin synthases from yeasts and fungi.

Authors:  José Ruiz-Herrera; Juan Manuel González-Prieto; Roberto Ruiz-Medrano
Journal:  FEMS Yeast Res       Date:  2002-01       Impact factor: 2.796

3.  csmA, a gene encoding a class V chitin synthase with a myosin motor-like domain of Aspergillus nidulans, is translated as a single polypeptide and regulated in response to osmotic conditions.

Authors:  Norio Takeshita; Akinori Ohta; Hiroyuki Horiuchi
Journal:  Biochem Biophys Res Commun       Date:  2002-10-18       Impact factor: 3.575

Review 4.  Chitin synthesis and inhibition: a revisit.

Authors:  E Cohen
Journal:  Pest Manag Sci       Date:  2001-10       Impact factor: 4.845

5.  WdChs4p, a homolog of chitin synthase 3 in Saccharomyces cerevisiae, alone cannot support growth of Wangiella (Exophiala) dermatitidis at the temperature of infection.

Authors:  Z Wang; L Zheng; M Hauser; J M Becker; P J Szaniszlo
Journal:  Infect Immun       Date:  1999-12       Impact factor: 3.441

Review 6.  Molecular genetic studies of the model dematiaceous pathogen Wangiella dermatitidis.

Authors:  Paul J Szaniszlo
Journal:  Int J Med Microbiol       Date:  2002-10       Impact factor: 3.473

7.  WdChs2p, a class I chitin synthase, together with WdChs3p (class III) contributes to virulence in Wangiella (Exophiala) dermatitidis.

Authors:  Z Wang; L Zheng; H Liu; Q Wang; M Hauser; S Kauffman; J M Becker; P J Szaniszlo
Journal:  Infect Immun       Date:  2001-12       Impact factor: 3.441

Review 8.  Dynamics of cell wall structure in Saccharomyces cerevisiae.

Authors:  Frans M Klis; Pieternella Mol; Klaas Hellingwerf; Stanley Brul
Journal:  FEMS Microbiol Rev       Date:  2002-08       Impact factor: 16.408

9.  Wangiella (Exophiala) dermatitidis WdChs5p, a class V chitin synthase, is essential for sustained cell growth at temperature of infection.

Authors:  Hongbo Liu; Sarah Kauffman; Jeffrey M Becker; Paul J Szaniszlo
Journal:  Eukaryot Cell       Date:  2004-02

10.  Transcription and expression analyses of WdCHS5, which encodes a class V chitin synthase with a myosin motor-like domain in Wangiella (Exophiala) dermatitidis.

Authors:  Hongbo Liu; Paul J Szaniszlo
Journal:  FEMS Microbiol Lett       Date:  2007-11       Impact factor: 2.742

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  2 in total

Review 1.  Black yeasts and their filamentous relatives: principles of pathogenesis and host defense.

Authors:  Seyedmojtaba Seyedmousavi; Mihai G Netea; Johan W Mouton; Willem J G Melchers; Paul E Verweij; G Sybren de Hoog
Journal:  Clin Microbiol Rev       Date:  2014-07       Impact factor: 26.132

2.  Expression in E. coli and characterization of the catalytic domain of Botrytis cinerea chitin synthase.

Authors:  Hervé Magellan; Thierry Drujon; Annie Thellend; Annie Piffeteau; Hubert F Becker
Journal:  BMC Res Notes       Date:  2010-11-11
  2 in total

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