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Open AccessArticle

Proteomic Characterization of Antibiotic Resistance, and Production of Antimicrobial and Virulence Factors in Streptococcus Species Associated with Bovine Mastitis. Could Enzybiotics Represent Novel Therapeutic Agents Against These Pathogens?

1
Departamento de Microbiología y Parasitología, Facultad de Farmacia, Campus Sur 15782, Universidad de Santiago de Compostela, 15705 Santiago de Compostela, Spain
2
Marine Research Institute (IIM), Spanish National Research Council (CSIC), Eduardo Cabello 6, 36208 Vigo, Pontevedra, Spain
3
Agroalimentary Technological Center of Lugo, Montirón 154, 27002 Lugo, Spain
4
Departamento de Química Analítica, Nutrición y Bromatología, Area de Tecnología de los Alimentos, Facultad de Veterinaria, Campus Lugo, Universidad de Santiago de Compostela, 27002 Lugo, Spain
5
Sydney School of Veterinary Science, Faculty of Science, University of Sydney, Sydney, NSW 2006, Australia
*
Author to whom correspondence should be addressed.
Antibiotics 2020, 9(6), 302; https://doi.org/10.3390/antibiotics9060302
Received: 4 May 2020 / Revised: 28 May 2020 / Accepted: 3 June 2020 / Published: 4 June 2020
(This article belongs to the Special Issue Phage Therapy, Lysin Therapy, and Antibiotics, a Trio Due to Come)
Streptococcus spp. are major mastitis pathogens present in dairy products, which produce a variety of virulence factors that are involved in streptococcal pathogenicity. These include neuraminidase, pyrogenic exotoxin, and M protein, and in addition they might produce bacteriocins and antibiotic-resistance proteins. Unjustifiable misuse of antimicrobials has led to an increase in antibiotic-resistant bacteria present in foodstuffs. Identification of the mastitis-causing bacterial strain, as well as determining its antibiotic resistance and sensitivity is crucial for effective therapy. The present work focused on the LC–ESI–MS/MS (liquid chromatography–electrospray ionization tandem mass spectrometry) analysis of tryptic digestion peptides from mastitis-causing Streptococcus spp. isolated from milk. A total of 2706 non-redundant peptides belonging to 2510 proteins was identified and analyzed. Among them, 168 peptides were determined, representing proteins that act as virulence factors, toxins, anti-toxins, provide resistance to antibiotics that are associated with the production of lantibiotic-related compounds, or play a role in the resistance to toxic substances. Protein comparisons with the NCBI database allowed the identification of 134 peptides as specific to Streptococcus spp., while two peptides (EATGNQNISPNLTISNAQLNLEDKNK and DLWC*NM*IIAAK) were found to be species-specific to Streptococcus dysgalactiae. This proteomic repository might be useful for further studies and research work, as well as for the development of new therapeutics for the mastitis-causing Streptococcus strains. View Full-Text
Keywords: LC–ESI–MS/MS; proteomics; mass spectrometry; characterization of antibiotic resistance peptides; lantibiotic production; virulence factors; Streptococcus spp. LC–ESI–MS/MS; proteomics; mass spectrometry; characterization of antibiotic resistance peptides; lantibiotic production; virulence factors; Streptococcus spp.
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Abril, A.G.; Carrera, M.; Böhme, K.; Barros-Velázquez, J.; Rama, J.-L.R.; Calo-Mata, P.; Sánchez-Pérez, A.; Villa, T.G. Proteomic Characterization of Antibiotic Resistance, and Production of Antimicrobial and Virulence Factors in Streptococcus Species Associated with Bovine Mastitis. Could Enzybiotics Represent Novel Therapeutic Agents Against These Pathogens? Antibiotics 2020, 9, 302.

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