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Evaluation of the Proline-Rich Antigen of Coccidioides immitis as a Vaccine Candidate in Mice
, 1998
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PCR assays for identification of Coccidioides posadasii based on the nucleotide sequence of the antigen 2/proline-rich
, 2004
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The structure of an allosamidin complex with the Coccidioides immitis chitinase defines a role for a second acid residue in substrate-assisted mechanism
- J. Mol. Biol
, 2002
"... Allosamidin is a known inhibitor of class 18 chitinases. We show that allosamidin is a competitive inhibitor of the fungal chitinase CiX1 from Coccidioides immitis, with a Ki of 60 nM. We report the X-ray structure of the complex and show that upon inhibitor binding the side-chain of Asp169 rotates ..."
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Allosamidin is a known inhibitor of class 18 chitinases. We show that allosamidin is a competitive inhibitor of the fungal chitinase CiX1 from Coccidioides immitis, with a Ki of 60 nM. We report the X-ray structure of the complex and show that upon inhibitor binding the side-chain of Asp169 rotates to form an ion pair with the oxazolinium cation. The mechanism of action is thought to involve protonation of the leaving group by Glu171 and substrate assistance by the sugar acetamido moiety to form an oxazoline-like intermediate. We converted both amino acid residues to the corresponding amide and found that each mutation effec-tively abolishes enzyme activity. X-ray structures show the mutant enzymes retain the basic wild-type structure and that the loss of mutant activity is due to their altered chemical properties. The high affinity of allosamidin, and its similarity to the putative reaction intermediate, suggests it is a transition state analog. This helps validate our contention that the role of Asp169 is to electrostatically stabilize the reaction transition state.
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, 2011
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This article cites 42 articles, 15 of which can be accessed free
Mapping of a Coccidioides immitis-specific epitope that reacts with complement-fixing antibody. Infect. Immun
, 1997
"... epitope that reacts with complement-fixing antibody. ..."
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epitope that reacts with complement-fixing antibody.
Recombinant Antigen 2 and Antigen 2 cDNA
, 1998
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REVIEW Glycosidase inhibitors: update and perspectives on practical use
, 2003
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Copyright © 2000 The Protein Society The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis
, 1999
"... The X-ray structure of chitinase from the fungal pathogen Coccidioides immitis has been solved to 2.2 Å resolution. Like other members of the class 18 hydrolase family, this 427 residue protein is an eight-stranded b0a-barrel. Although lacking an N-terminal chitin anchoring domain, the enzyme closel ..."
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The X-ray structure of chitinase from the fungal pathogen Coccidioides immitis has been solved to 2.2 Å resolution. Like other members of the class 18 hydrolase family, this 427 residue protein is an eight-stranded b0a-barrel. Although lacking an N-terminal chitin anchoring domain, the enzyme closely resembles the chitinase from Serratia marcescens. Among the conserved features are three cis peptide bonds, all involving conserved active site residues. The active site
Copyright © 1997, American Society for Microbiology Prospects for the Development of Fungal Vaccines
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