Isolation and Molecular Characterization of Catalase-Negative <i>Staphylococcus aureus</i> from Sputum of a Patient with Aspiration Pneumonia

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  • Horiuchi Kazuki
    Department of Laboratory Medicine, Shinshu University Hospital
  • Matsumoto Takehisa
    Department of Laboratory Medicine, Shinshu University Hospital
  • Hidaka Eiko
    Department of Laboratory Medicine, Shinshu University Hospital
  • Kasuga Eriko
    Department of Laboratory Medicine, Shinshu University Hospital
  • Sugano Mitsutoshi
    Department of Laboratory Medicine, Shinshu University Hospital
  • Oana Kozue
    Department of Biomedical Laboratory Sciences, School of Health Sciences, Shinshu University School of Medicine
  • Kawakami Yoshiyuki
    Department of Biomedical Laboratory Sciences, School of Health Sciences, Shinshu University School of Medicine
  • Honda Takayuki
    Department of Laboratory Medicine, Shinshu University Hospital

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  • Isolation and Molecular Characterization of Catalase-Negative Staphylococcus aureus from Sputum of a Patient with Aspiration Pneumonia

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Abstract

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.

Journal

  • Japanese Journal of Infectious Diseases

    Japanese Journal of Infectious Diseases 65 (5), 439-441, 2012

    National Institute of Infectious Diseases, Japanese Journal of Infectious Diseases Editorial Committee

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