Broad-spectrum resistance of Pseudomonas aeruginosa from shellfish: infrequent acquisition of novel resistance mechanisms

Environ Monit Assess. 2018 Jan 15;190(2):81. doi: 10.1007/s10661-018-6471-3.

Abstract

Pseudomonas aeruginosa is one the most common multidrug-resistant pathogens worldwide. It has been previously detected in marine shellfish, but its antibiotic resistance in such environment has not been explored. By combining PCR detection of acquired genes, and resistance-nodulation-cell division (RND) efflux studying, we investigated the multifactorial resistance traits of 108 P. aeruginosa isolates recovered from wild-growing Mediterranean mussels (Mytilus galloprovincialis) in Croatia. Eleven different resistance profiles were found, with the main mechanism being the overexpression of intrinsic efflux pump(s), particularly MexAB-OprM. Several acquired resistance determinants were detected, including the β-lactamase gene blaTEM-116, sulfamethoxazole resistance gene sul1, and the class 1 integron gene cassette carrying the streptomycin resistance gene aadA7. This study evidenced the multiple resistance in P. aeruginosa in shellfish from human-impacted marine environment, pointing to the underestimated role of the marine habitat for maintenance of multiresistant P. aeruginosa and, consequently, the potential risk for human and environmental health.

Keywords: ESBL; Efflux study; Marine environment; Mytilus galloprovincialis; Pseudomonas aeruginosa.

MeSH terms

  • Animals
  • Anti-Bacterial Agents / pharmacology
  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins / genetics
  • Croatia
  • Drug Resistance, Microbial / genetics*
  • Environmental Monitoring*
  • Humans
  • Membrane Transport Proteins
  • Microbial Sensitivity Tests
  • Mytilus / microbiology*
  • Polymerase Chain Reaction
  • Pseudomonas aeruginosa / genetics*
  • Shellfish
  • beta-Lactamases / genetics

Substances

  • Anti-Bacterial Agents
  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Membrane Transport Proteins
  • beta-Lactamases