Abstract:SummaryStaphylococcus epidermidis strains are diverse in their pathogenicity; some are invasive and cause serious nosocomial infections, whereas others are nonpathogenic commensal organisms. To analyse the implications of different virulence factors in Staphylococcus epidermidis infections, the complete genome of Staphylococcus epidermidis strain ATCC 12228, a non-biofilm forming, non-infection associated strain used for detection of residual antibiotics in food products, was sequenced. This strain showed low … Show more
“…The deduced amino acid sequence of AJ was 99.5 similar to that of V8 protease from S. epidermidis ATCC 12228 (Fig. 8) [23]. But, two proteins showed diVerent optimum pH Fig.…”
mentioning
confidence: 75%
“…AJ, Staphylococcus sp. strain AJ (this study); V8, from S. epidermidis ATCC 12228 [23]; glutamic, glutamic acidspeciWc endoprotease from S. aureus ATCC 12600 [24]; glutamyl, glutamyl endopeptidase from S. warneri M [25]. Underline indicates the N-terminal amino acid position of 11 kDa fragment of AJ Fig.…”
mentioning
confidence: 87%
“…The N-terminal amino acid sequence of the puriWed enzyme up to residue 17 was Val-Ile-Leu-Pro-Asn-Asn-XArg-His-Gln-Ile-Phe-X-Thr-Thr-Gln-Gly-, and shared a high degree of similarity with the N-terminal sequences of a glutamyl endopeptidase (also known as V8 serine protease) from S. epidermidis ATCC 12228 [23], S. aureus ATCC 12600 [24], and S. warneri M [25].…”
Section: N-terminal Amino Acid Sequence Of the Puriwed Enzymementioning
confidence: 99%
“…The nucleotide sequence revealed only one large open reading frame. The amino acid sequence of AJ was compared with the published sequences of the other proteins, and AJ was found to be identical to V8 protease from S. epidermidis ATCC 12228 [23], except for one amino acid substitution Ser44Asn (Fig. 8, arrow marked).…”
Section: N-terminal Amino Acid Sequence Of the Puriwed Enzymementioning
A novel Wbrinolytic enzyme (AJ) was puriWed from Staphylococcus sp. strain AJ screened from Korean salt-fermented Anchovy-jeot. Relative molecular weight of AJ was determined as 26 kDa by using SDS-PAGE and Wbrin zymography. Based on a 2D gel, AJ was found to consist of three active isoforms (pI 5.5-6.0) with the same N-terminal amino acid sequence. AJ exhibited optimum pH and temperature at 2.5-3.0 and 85°C, respectively. AJ kept 85% of the initial activity after heating at 100°C for 20 min on the zymogram gel. The Michaelis constant (K m ) and K cat values of AJ towards -casein were 0.38 mM and 19.73 s ¡1 , respectively. AJ cleaved the A -chain of Wbrinogen but did not aVect the B -and -chains, indicating that it is an -Wbrinogenase. The Wbrinolytic activity was inhibited by diisopropyl Xuorophosphate, indicating AJ is a serine protease. Interestingly, AJ was very stable at acidic condition, SDS, and heat (100°C), whereas it was easily degraded at neutral and alkaline conditions. In particular, AJ formed an active homo-dimer in the pH range from 7.0 to 8.0. To our knowledge, a similar combination of acid and heat stability has not yet been reported for other Wbrinolytic enzymes.
“…The deduced amino acid sequence of AJ was 99.5 similar to that of V8 protease from S. epidermidis ATCC 12228 (Fig. 8) [23]. But, two proteins showed diVerent optimum pH Fig.…”
mentioning
confidence: 75%
“…AJ, Staphylococcus sp. strain AJ (this study); V8, from S. epidermidis ATCC 12228 [23]; glutamic, glutamic acidspeciWc endoprotease from S. aureus ATCC 12600 [24]; glutamyl, glutamyl endopeptidase from S. warneri M [25]. Underline indicates the N-terminal amino acid position of 11 kDa fragment of AJ Fig.…”
mentioning
confidence: 87%
“…The N-terminal amino acid sequence of the puriWed enzyme up to residue 17 was Val-Ile-Leu-Pro-Asn-Asn-XArg-His-Gln-Ile-Phe-X-Thr-Thr-Gln-Gly-, and shared a high degree of similarity with the N-terminal sequences of a glutamyl endopeptidase (also known as V8 serine protease) from S. epidermidis ATCC 12228 [23], S. aureus ATCC 12600 [24], and S. warneri M [25].…”
Section: N-terminal Amino Acid Sequence Of the Puriwed Enzymementioning
confidence: 99%
“…The nucleotide sequence revealed only one large open reading frame. The amino acid sequence of AJ was compared with the published sequences of the other proteins, and AJ was found to be identical to V8 protease from S. epidermidis ATCC 12228 [23], except for one amino acid substitution Ser44Asn (Fig. 8, arrow marked).…”
Section: N-terminal Amino Acid Sequence Of the Puriwed Enzymementioning
A novel Wbrinolytic enzyme (AJ) was puriWed from Staphylococcus sp. strain AJ screened from Korean salt-fermented Anchovy-jeot. Relative molecular weight of AJ was determined as 26 kDa by using SDS-PAGE and Wbrin zymography. Based on a 2D gel, AJ was found to consist of three active isoforms (pI 5.5-6.0) with the same N-terminal amino acid sequence. AJ exhibited optimum pH and temperature at 2.5-3.0 and 85°C, respectively. AJ kept 85% of the initial activity after heating at 100°C for 20 min on the zymogram gel. The Michaelis constant (K m ) and K cat values of AJ towards -casein were 0.38 mM and 19.73 s ¡1 , respectively. AJ cleaved the A -chain of Wbrinogen but did not aVect the B -and -chains, indicating that it is an -Wbrinogenase. The Wbrinolytic activity was inhibited by diisopropyl Xuorophosphate, indicating AJ is a serine protease. Interestingly, AJ was very stable at acidic condition, SDS, and heat (100°C), whereas it was easily degraded at neutral and alkaline conditions. In particular, AJ formed an active homo-dimer in the pH range from 7.0 to 8.0. To our knowledge, a similar combination of acid and heat stability has not yet been reported for other Wbrinolytic enzymes.
“…Bacterial strains which had previously been characterized for their biofilm formation capacity, i.e. Staphylococcus aureus SC08 and S. epidermidis ATCC 12228 [33], served as the positive and negative controls, respectively.Figure 3.Mammoth Mountain Permafrost 1 (MMP1, Staphylococcus warneri ) and MMP2 ( Staphylococcus hominis ) can form biofilms. (A) Colony morphology of bacteria on Congo red agar plates.…”
Background: Permafrost preserves a variety of viable ancient microorganisms. Some of them can be cultivated after being kept at subzero temperatures for thousands or even millions of years.Objective: To cultivate bacterial strains from permafrost.Design: We isolated and cultivated two bacterial strains from permafrost that was obtained at Mammoth Mountain in Siberia and attributed to the Middle Miocene. Bacterial genomic DNA was sequenced with 40–60× coverage and high-quality contigs were assembled. The first strain was assigned to Staphylococcus warneri species (designated MMP1) and the second one to Staphylococcus hominis species (designated MMP2), based on the classification of 16S ribosomal RNA genes and genomic sequences.Results: Genomic sequence analysis revealed the close relation of the isolated ancient bacteria to the modern bacteria of this species. Moreover, several genes associated with resistance to different groups of antibiotics were found in the S. hominis MMP2 genome.Conclusions: These findings supports a hypothesis that antibiotic resistance has an ancient origin. The enrichment of cultivated bacterial communities with ancient permafrost strains is essential for the analysis of bacterial evolution and antibiotic resistance.
The staphylococci are opportunistic pathogens and a major cause of hospital‐ and community‐acquired infections ranging in severity from minor skin infections to widespread life‐threatening infections. The occurrence of highly virulent community‐acquired
Staphylococcus aureus
(CASA) and continued progression of resistance to multiple antimicrobials, including vancomycin, marks a re‐emergence of the staphylococci as serious health care threat. Multiple genomes of the two major staphylococcal pathogens,
S. aureus
and
Staphylococcus epidermidis
, have been sequenced (genomes of seven
S. aureus
isolates and two
S. epidermidis
isolates). Comparative analysis of these genomes has shown that they are syntenic along their length and share a core set of genes with roles in metabolism and general housekeeping functions. Nonsyntenic regions contain species‐specific genes and pathogenicity genomic islands, including bacteriophages, which are the primary source of variations in pathogenicity and resistance. Overall differences in pathogenicity between the two species can be attributed to genome islands in
S. aureus
, which encode exotoxins, leukocidins, and leukotoxins not found in
S. epidermidis
. Gene transfer among staphylococci and with other low GC gram‐positive bacteria has contributed to the evolution of resistance and virulence and is likely playing a role in the emergence of increasingly virulent members of the staphylococcal family.
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