Lipase and Protease Production Ability of Multi-drug Resistant Bacteria Worsens the Outcomes of Wound Infections


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Abstract

Background:Surgical site infections are one of the major clinical problems in surgical departments that cost hundreds of millions of dollars to healthcare systems around the world.

Aim:The study aimed to address the pressing issue of surgical site infections, which pose significant clinical and financial burdens on healthcare systems globally. Recognizing the substantial costs incurred due to these infections, the research has focused on understanding the role of lipase and protease production by multi-drug resistant bacteria isolated from surgical wounds in the development of post-surgical wound infections.

Methods:For these purposes, 153 pus specimens were collected from patients with severe post-surgical wound infections having prolonged hospital stays. The specimens were inoculated on appropriate culture media. Gram staining and biochemical tests were used for the identification of bacterial growth on suitable culture media after 24 hours of incubation. The isolated pathogens were then applied for lipase and protease, key enzymes that could contribute to wound development, on tributyrin and skimmed milk agar, respectively. Following the CSLI guidelines, the Kirby-Bauer disc diffusion method was used to assess antibiotic susceptibility patterns. The results revealed that a significant proportion of the samples (127 out of 153) showed bacterial growth of Gram-negative (n = 66) and Gram-positive (n = 61) bacteria. In total, isolated 37 subjects were declared MDR due to their resistance to three or more than three antimicrobial agents. The most prevalent bacteria were Staphylococcus aureus (29.13%), followed by S. epidermidis (18.89%), Klebsiella pneumoniae (18.89%), Escherichia coli (14.96%), Pseudomonas aeruginosa (10.23%), and Proteus mirabilis (7.87%). Moreover, a considerable number of these bacteria exhibited lipase and protease activity with 70 bacterial strains as lipase positive on tributyrin agar, whereas 74 bacteria showed protease activity on skimmed milk agar with P. aeruginosa as the highest lipase (69.23%) and protease (76.92%) producer, followed by S. aureus (lipase 62.16% and protease 70.27%).

Results:The antimicrobial resistance was evaluated among enzyme producers and non-producers and it was found that the lipase and protease-producing bacteria revealed higher resistance to selected antibiotics than non-producers. Notably, fosfomycin and carbapenem were identified as effective antibiotics against the isolated bacterial strains. However, gram-positive bacteria displayed high resistance to lincomycin and clindamycin, while gram-negative bacteria were more resistant to cefuroxime and gentamicin.

Conclusion:In conclusion, the findings suggest that lipases and proteases produced by bacteria could contribute to drug resistance and act as virulence factors in the development of surgical site infections. Understanding the role of these enzymes may inform strategies for preventing and managing post-surgical wound infections more effectively.

About the authors

Attaur Rahman

Laboratório de Hanseníase, Department of Parasitology, Institute Oswaldo Cruz-Fiocruz

Email: info@benthamscience.net

Saiqa Sardar

Malaria Research Laboratory, Departament of Parasitology, Institute Oswaldo Cruz-Fiocruz

Email: info@benthamscience.net

Zeeshan Niaz

Department of Microbiology, Hazara University

Email: info@benthamscience.net

Asif Khan

Laboratory of Phytochemistry, Department of Botany, University of Sao Paulo

Email: info@benthamscience.net

Sheheryar Sheheryar

Department of Biochemistry and Molecular Biology,, Federal University of Ceara

Author for correspondence.
Email: info@benthamscience.net

Abdulwahed Alrefaei

Department of Zoology, College of Science, King Saud University

Email: info@benthamscience.net

Muhammad Hamayun

Department of Botany, Abdul Wali Khan University Mardan

Email: info@benthamscience.net

Sajid Ali

Department of Horticulture and Life Science, Yeungnam University

Author for correspondence.
Email: info@benthamscience.net

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