scholarly journals Proteomic Characterization of Bacteriophage Peptides from the Mastitis Producer Staphylococcus aureus by LC-ESI-MS/MS and the Bacteriophage Phylogenomic Analysis

Foods ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 799
Author(s):  
Ana G. Abril ◽  
Mónica Carrera ◽  
Karola Böhme ◽  
Jorge Barros-Velázquez ◽  
Benito Cañas ◽  
...  

The present work describes LC-ESI-MS/MS MS (liquid chromatography-electrospray ionization-tandem mass spectrometry) analyses of tryptic digestion peptides from phages that infect mastitis-causing Staphylococcus aureus isolated from dairy products. A total of 1933 nonredundant peptides belonging to 1282 proteins were identified and analyzed. Among them, 79 staphylococcal peptides from phages were confirmed. These peptides belong to proteins such as phage repressors, structural phage proteins, uncharacterized phage proteins and complement inhibitors. Moreover, eighteen of the phage origin peptides found were specific to S. aureus strains. These diagnostic peptides could be useful for the identification and characterization of S. aureus strains that cause mastitis. Furthermore, a study of bacteriophage phylogeny and the relationship among the identified phage peptides and the bacteria they infect was also performed. The results show the specific peptides that are present in closely related phages and the existing links between bacteriophage phylogeny and the respective Staphylococcus spp. infected.

Author(s):  
Sejal S. Chaudhary ◽  
Harshad C. Chauhan ◽  
Kishan Kumar Sharma ◽  
Sandip S. Patel ◽  
Sushil Kumar Mohapatra ◽  
...  

Background: The present study was done to ascertain prevalence of Staphylococcus aureus from various canine affections in Banaskantha district of Gujarat, India. Along with this, use of classical and molecular techniques were compared in identification and virulence characterization of this pathogen.Methods: A total of 165 samples were collected and bacterial identification was carried out with bacteriological (phenotypic) techniques and confirmed by genus specific 16S rDNA and Staphylococcus aureus specific sa442 gene based PCR. Isolates were characterized for coagulase production, haemolysis activity and presence of spa gene. Result: Samples yielded, 88 (53.33%) Staphylococcus spp. via bacteriological and PCR methods. Clinically, 19 (21.59%), 28 (31.82%), 12 (13.64%), 15 (17.04%) and 14 (15.91%) isolates were from abscess/wound, pyoderma, respiratory problems, eye infections and Otitis, respectively. A total of 46/88 (52.27%) isolates were confirmed as Staphylococcus aureus in PCR. In tube coagulase test, 51/88 (57.95%) isolates were found positive. A tota of 42 isolates revealed presence of coa gene, including two tube coagulase negative isolates. Haemolytic activity revealed beta (51.14%) gamma (31.82%), alpha (13.64%) and alpha-beta (3.41%) haemolysis, respectively. X-region of Protein A (spa gene) was detected in 26 /46 (56.52%) isolates in PCR.


2018 ◽  
Vol 308 (4) ◽  
pp. 438-446 ◽  
Author(s):  
Dao-Feng Zhang ◽  
Xin-Yi Yang ◽  
Jing Zhang ◽  
Xiaojie Qin ◽  
Xiaozhen Huang ◽  
...  

2018 ◽  
Vol 08 (06) ◽  
Author(s):  
Zobayda Farzana Haque ◽  
Abdullah Al Momen Sabuj ◽  
Md. Muket Mahmud ◽  
Amrita Pondit ◽  
Md. Ariful Islam ◽  
...  

1987 ◽  
Vol 243 (1) ◽  
pp. 309-312 ◽  
Author(s):  
H K Young ◽  
R A Skurray ◽  
S G B Amyes

The trimethoprim-resistance gene located on plasmid pSK1, originally identified in a multi-resistant Staphylococcus aureus from Australia, encodes the production of a dihydrofolate reductase (type S1), which confers a high degree of resistance to its host and is quite unlike any plasmid-encoded dihydrofolate reductase hitherto described. It has a low Mr (19,700) and has a higher specific activity than the constitutive Gram-negative plasmid dihydrofolate reductases. The type S1 enzyme is heat-stable and has a relatively low affinity for the substrate, dihydrofolate (Km 10.8 microM). It is moderately resistant to trimethoprim, and is competitively inhibited by this drug with an inhibitor-binding constant of 11.6 microM. This is the first identification and characterization of a plasmid-encoded trimethoprim-resistant dihydrofolate reductase derived from a Gram-positive species.


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