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Proteomics As a Tool for Studying Bacterial Virulence and Antimicrobial Resistance.

Pérez-Llarena FJ, Bou G - Front Microbiol (2016)

Bottom Line: Proteomic studies have improved our understanding of the microbial world.This review article addresses these issues in some of the most important human pathogens.It also reports some applications of Matrix-Assisted Laser Desorption/Ionization-Time-Of-Flight (MALDI-TOF) mass spectrometry that may be important for the diagnosis of bacterial resistance in clinical laboratories in the future.

View Article: PubMed Central - PubMed

Affiliation: Servicio de Microbiología-INIBIC, Complejo Hospitalario Universitario A Coruña A Coruña, Spain.

ABSTRACT
Proteomic studies have improved our understanding of the microbial world. The most recent advances in this field have helped us to explore aspects beyond genomics. For example, by studying proteins and their regulation, researchers now understand how some pathogenic bacteria have adapted to the lethal actions of antibiotics. Proteomics has also advanced our knowledge of mechanisms of bacterial virulence and some important aspects of how bacteria interact with human cells and, thus, of the pathogenesis of infectious diseases. This review article addresses these issues in some of the most important human pathogens. It also reports some applications of Matrix-Assisted Laser Desorption/Ionization-Time-Of-Flight (MALDI-TOF) mass spectrometry that may be important for the diagnosis of bacterial resistance in clinical laboratories in the future. The reported advances will enable new diagnostic and therapeutic strategies to be developed in the fight against some of the most lethal bacteria affecting humans.

No MeSH data available.


Related in: MedlinePlus

Differentiation between different β-lactamase subgroups and species. (A) Phylogenetic tree based on a sequence alignment of different β-lactamases from different functional subgroups. For some classes, the primary structures are very similar (e.g., KPC and CTX) while for others, individual sequences vary considerably (e.g., OXA). (B) Tandem mass spectrum for a unique tryptic peptide from the KPC-group of carbapenemases (FPLCSSFK). (C) Tandem mass spectrum for a unique tryptic peptide from OXA-48 (SQGVVVLWNENK). Obtained and adapted from Fleurbaaij et al. (2014) and reprinted with permission from the publisher.
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Figure 2: Differentiation between different β-lactamase subgroups and species. (A) Phylogenetic tree based on a sequence alignment of different β-lactamases from different functional subgroups. For some classes, the primary structures are very similar (e.g., KPC and CTX) while for others, individual sequences vary considerably (e.g., OXA). (B) Tandem mass spectrum for a unique tryptic peptide from the KPC-group of carbapenemases (FPLCSSFK). (C) Tandem mass spectrum for a unique tryptic peptide from OXA-48 (SQGVVVLWNENK). Obtained and adapted from Fleurbaaij et al. (2014) and reprinted with permission from the publisher.

Mentions: Detection of antibiotic resistance markers, such as peptide fragments, in clinical strains of E. coli associated with some beta-lactamases (CTX-M1, CMY-2, VIM, and TEM) together with kanR and aminoglycoside modifying enzyme was obtained by periplasm extraction followed by nano-LC separation (Hart et al., 2015) Capillary-electrophoresis mass spectrometry is useful for detecting OXA-48 and KPC carbapenemases in multi-drug resistant Gram-negative bacteria (Fleurbaaij et al., 2014; Figure 2), and detection of beta-lactamase proteins has been improved by the use of MALDI-TOF MS methods rather than PCR detection of the corresponding genes (Trip et al., 2015).


Proteomics As a Tool for Studying Bacterial Virulence and Antimicrobial Resistance.

Pérez-Llarena FJ, Bou G - Front Microbiol (2016)

Differentiation between different β-lactamase subgroups and species. (A) Phylogenetic tree based on a sequence alignment of different β-lactamases from different functional subgroups. For some classes, the primary structures are very similar (e.g., KPC and CTX) while for others, individual sequences vary considerably (e.g., OXA). (B) Tandem mass spectrum for a unique tryptic peptide from the KPC-group of carbapenemases (FPLCSSFK). (C) Tandem mass spectrum for a unique tryptic peptide from OXA-48 (SQGVVVLWNENK). Obtained and adapted from Fleurbaaij et al. (2014) and reprinted with permission from the publisher.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4814472&req=5

Figure 2: Differentiation between different β-lactamase subgroups and species. (A) Phylogenetic tree based on a sequence alignment of different β-lactamases from different functional subgroups. For some classes, the primary structures are very similar (e.g., KPC and CTX) while for others, individual sequences vary considerably (e.g., OXA). (B) Tandem mass spectrum for a unique tryptic peptide from the KPC-group of carbapenemases (FPLCSSFK). (C) Tandem mass spectrum for a unique tryptic peptide from OXA-48 (SQGVVVLWNENK). Obtained and adapted from Fleurbaaij et al. (2014) and reprinted with permission from the publisher.
Mentions: Detection of antibiotic resistance markers, such as peptide fragments, in clinical strains of E. coli associated with some beta-lactamases (CTX-M1, CMY-2, VIM, and TEM) together with kanR and aminoglycoside modifying enzyme was obtained by periplasm extraction followed by nano-LC separation (Hart et al., 2015) Capillary-electrophoresis mass spectrometry is useful for detecting OXA-48 and KPC carbapenemases in multi-drug resistant Gram-negative bacteria (Fleurbaaij et al., 2014; Figure 2), and detection of beta-lactamase proteins has been improved by the use of MALDI-TOF MS methods rather than PCR detection of the corresponding genes (Trip et al., 2015).

Bottom Line: Proteomic studies have improved our understanding of the microbial world.This review article addresses these issues in some of the most important human pathogens.It also reports some applications of Matrix-Assisted Laser Desorption/Ionization-Time-Of-Flight (MALDI-TOF) mass spectrometry that may be important for the diagnosis of bacterial resistance in clinical laboratories in the future.

View Article: PubMed Central - PubMed

Affiliation: Servicio de Microbiología-INIBIC, Complejo Hospitalario Universitario A Coruña A Coruña, Spain.

ABSTRACT
Proteomic studies have improved our understanding of the microbial world. The most recent advances in this field have helped us to explore aspects beyond genomics. For example, by studying proteins and their regulation, researchers now understand how some pathogenic bacteria have adapted to the lethal actions of antibiotics. Proteomics has also advanced our knowledge of mechanisms of bacterial virulence and some important aspects of how bacteria interact with human cells and, thus, of the pathogenesis of infectious diseases. This review article addresses these issues in some of the most important human pathogens. It also reports some applications of Matrix-Assisted Laser Desorption/Ionization-Time-Of-Flight (MALDI-TOF) mass spectrometry that may be important for the diagnosis of bacterial resistance in clinical laboratories in the future. The reported advances will enable new diagnostic and therapeutic strategies to be developed in the fight against some of the most lethal bacteria affecting humans.

No MeSH data available.


Related in: MedlinePlus