Isolation and Molecular Characterization of Catalase-Negative Staphylococcus aureus from Sputum of a Patient with Aspiration Pneumonia
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- Horiuchi Kazuki
- Department of Laboratory Medicine, Shinshu University Hospital
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- Matsumoto Takehisa
- Department of Laboratory Medicine, Shinshu University Hospital
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- Hidaka Eiko
- Department of Laboratory Medicine, Shinshu University Hospital
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- Kasuga Eriko
- Department of Laboratory Medicine, Shinshu University Hospital
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- Sugano Mitsutoshi
- Department of Laboratory Medicine, Shinshu University Hospital
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- Oana Kozue
- Department of Biomedical Laboratory Sciences, School of Health Sciences, Shinshu University School of Medicine
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- Kawakami Yoshiyuki
- Department of Biomedical Laboratory Sciences, School of Health Sciences, Shinshu University School of Medicine
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- Honda Takayuki
- Department of Laboratory Medicine, Shinshu University Hospital
書誌事項
- タイトル別名
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- Isolation and Molecular Characterization of Catalase-Negative <i>Staphylococcus aureus</i> from Sputum of a Patient with Aspiration Pneumonia
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抄録
Staphylococcus aureus produces various virulence factors. The catalase enzyme, in particular, is considered to be involved in oxidative stress resistance, and catalase activity is an important criterion for differentiating staphylococci from streptococci. In this report, we describe the catalase-negative S. aureus strain SH3064, which was isolated from the sputum of a patient with aspiration pneumonia. To evaluate the causes of the lack of catalase activity in S. aureus SH3064, we analyzed the sequence of katA gene encoding the catalase enzyme in this strain. We amplified the complete sequence of katA gene of S. aureus SH3064 by polymerase chain reaction using 2 sets of primers. The katA sequence showed 99.6% sequence identity (1512/1518 bp) with that of S. aureus ATCC 12600. We detected 2 mutations in the katA gene from S. aureus SH3064, an A217T substitution leading to a threonine 73-to-serine substitution and a single-base pair deletion (c.637delG) resulting in a frameshift mutation. The lack of catalase activity in this strain was attributed to the shift of the nucleotide reading frame.
収録刊行物
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- Japanese Journal of Infectious Diseases
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Japanese Journal of Infectious Diseases 65 (5), 439-441, 2012
国立感染症研究所 Japanese Journal of Infectious Diseases 編集委員会
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詳細情報 詳細情報について
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- CRID
- 1390282681218012672
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- NII論文ID
- 130001931857
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- NII書誌ID
- AA1132885X
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- ISSN
- 18842836
- 13446304
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- HANDLE
- 10091/17631
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- NDL書誌ID
- 023971675
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- PubMed
- 22996221
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- IRDB
- NDL
- Crossref
- PubMed
- CiNii Articles
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