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Section Microbiology

Molecular Study of Lysozyme Resistant Gram- negative Bacteria

Vol. 10 No. 2 (2025): December:

Hussain Adnan Hashim (1)

(1) Department of Pathological Analysis, College of Science, University of Thi-Qar, Iraq
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Abstract:

General Background: Lysozyme, an essential antimicrobial enzyme found in bodily fluids, serves as a vital component of the innate immune system, acting primarily by hydrolyzing bacterial cell walls. Specific Background: While lysozyme effectively targets Gram-positive bacteria, Gram-negative bacteria often display resistance due to their protective outer membrane. Recent studies have suggested that specific genes, such as icaA and OatA, may contribute to lysozyme resistance by enhancing biofilm formation and altering cell wall structure. Knowledge Gap: Limited molecular data exist regarding the prevalence of these resistance genes among Gram-negative pathogens isolated from burn patients, particularly in Iraq. Aims: This study aimed to identify the presence of icaA and OatA genes in Gram-negative bacterial isolates from burn patients and assess their potential roles in lysozyme resistance. Results: Among 36 bacterial isolates, Pseudomonas aeruginosa (72.20%) and Klebsiella pneumoniae (27.80%) were dominant. The icaA gene was detected in 30.60% and the OatA gene in 22.20% of isolates. Novelty: This research provides the first molecular evidence of icaA and OatA gene distribution among lysozyme-resistant Gram-negative bacteria in burn patients in Thi-Qar. Implications: The findings highlight the need for continuous molecular surveillance of resistance determinants to improve antimicrobial strategies and infection control in burn treatment settings.
Highlight :




  • Lysozyme is a key natural antibacterial enzyme.




  • icaA and OatA genes were found in burn bacterial isolates.




  • Monitoring resistance genes is essential.




Keywords : Pseudomonas Aeruginosa, OatA Gene, icaA Gene, Burn Patient, Lysozyme Resistant

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References

T. V. Tullio, R. Spaccapelo, and M. Polimeni, "Lysozymes in the Animal Kingdom," in Human and Mosquito Lysozymes: Old Molecules for New Approaches Against Malaria, Cham, Switzerland: Springer International Publishing, 2014, pp. 45–57.

I. S. Vavilina, A. A. Shpak, T. A. Druzhkova, A. B. Guekht, and N. V. Gulyaeva, "Shedding Valuable Tears: Tear Fluid as a Promising Source of Disease Biomarkers," Neurochemical Journal, vol. 17, no. 4, pp. 702–714, Dec. 2023, doi: 10.1134/S1819712423040121.

N. Nawaz, S. Wen, F. Wang, S. Nawaz, J. Raza, M. Iftikhar, and M. Usman, "Lysozyme and Its Application as Antibacterial Agent in Food Industry," Molecules, vol. 27, no. 19, p. 6305, Sep. 2022, doi: 10.3390/molecules27196305.

K. H. Nam, "Crystal Structure of Human Lysozyme Complexed with N-Acetyl-α-D-Glucosamine," Applied Sciences, vol. 12, no. 9, p. 4363, Apr. 2022, doi: 10.3390/app12094363.

T. Yang and W. Yan, "Strategies for Enhancing the Antibacterial Efficacy of Lysozyme and the Resulting Outcome," International Journal of Biological Macromolecules, vol. 143, pp. 137–146, Apr. 2025, doi: 10.1016/j.ijbiomac.2025.04.137.

K. Skrzyniarz, J. Sanchez-Nieves, F. J. de la Mata, M. Lysek-Gladysinska, K. Lach, and K. Ciepluch, "Mechanistic Insight of Lysozyme Transport Through the Outer Bacteria Membrane with Dendronized Silver Nanoparticles for Peptidoglycan Degradation," International Journal of Biological Macromolecules, vol. 237, p. 124239, May 2023, doi: 10.1016/j.ijbiomac.2023.124239.

P. Biswas, G. Mukherjee, J. Singh, A. Rastogi, and R. Banerjee, "Enzymes in Health Care: Cost-Effective Production and Applications of Therapeutic Enzymes in Health Care Sector," in Bioprospecting of Enzymes in Industry, Healthcare and Sustainable Environment, Singapore: Springer Singapore, 2021, pp. 291–314.

A. Rkhaila, T. Chtouki, H. Erguig, N. El Haloui, and K. Ounine, "Chemical Properties of Biopolymers (Chitin/Chitosan) and Their Synergic Effects with Endophytic Bacillus Species: Unlimited Applications in Agriculture," Molecules, vol. 26, no. 4, p. 1117, Feb. 2021, doi: 10.3390/molecules26041117.

D. A. Heesterbeek et al., "Outer Membrane Permeabilization by the Membrane Attack Complex Sensitizes Gram-Negative Bacteria to Antimicrobial Proteins in Serum and Phagocytes," PLoS Pathogens, vol. 17, no. 1, p. e1009227, Jan. 2021, doi: 10.1371/journal.ppat.1009227.

P. Ferraboschi, S. Ciceri, and P. Grisenti, "Applications of Lysozyme, an Innate Immune Defense Factor, as an Alternative Antibiotic," Antibiotics, vol. 10, no. 12, p. 1534, Dec. 2021, doi: 10.3390/antibiotics10121534.

V. C. Oliveira et al., "Characterization of a Peptidoglycan-Degrading Protein: Biochemical and Antimicrobial Characteristics, Antibiotic Synergism, and Delivery System Innovation," Probiotics and Antimicrobial Proteins, vol. 1, no. 2, Oct. 2024, doi: 10.1007/s12602-024-01345-8.

H. Fadhil, "Association Between the Demographic Characteristics of Patients and the Severity of COVID-19," University of Thi-Qar Journal of Science, vol. 10, no. 2, pp. 92–97, Dec. 2023.

P. Ferraboschi, S. Ciceri, and P. Grisenti, "Applications of Lysozyme, an Innate Immune Defense Factor, as an Alternative Antibiotic," Antibiotics, vol. 10, no. 12, p. 1534, Dec. 2021, doi: 10.3390/antibiotics10121534.

A. Elfadadny et al., "Antimicrobial Resistance of Pseudomonas Aeruginosa: Navigating Clinical Impacts, Current Resistance Trends, and Innovations in Breaking Therapies," Frontiers in Microbiology, vol. 15, p. 1374466, Apr. 2024, doi: 10.3389/fmicb.2024.1374466.

T. Nuryastuti, H. C. van der Mei, H. J. Busscher, S. Iravati, A. T. Aman, and B. P. Krom, "Effect of Cinnamon Oil on icaA Expression and Biofilm Formation by Staphylococcus Epidermidis," Applied and Environmental Microbiology, vol. 75, no. 21, pp. 6850–6855, Nov. 2009, doi: 10.1128/AEM.00875-09.

A. Bera, S. Herbert, A. Jakob, W. Vollmer, and F. Gotz, "Why Are Pathogenic Staphylococci So Lysozyme Resistant? The Peptidoglycan O-Acetyltransferase OatA Is the Major Determinant for Lysozyme Resistance of Staphylococcus Aureus," Molecular Microbiology, vol. 55, no. 3, pp. 778–787, Feb. 2005, doi: 10.1111/j.1365-2958.2004.04429.x.