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High prevalence of blaVEB, blaGES and blaPER genes in beta-lactam resistant clinical isolates of Pseudomonas aeruginosa

  • Received: 07 March 2022 Revised: 12 April 2022 Accepted: 20 April 2022 Published: 25 April 2022
  • The increased prevalence of β-lactamase is one of the main factors in resistance to β-lactams in Pseudomonas aeruginosa. This study aimed to investigate the prevalence of blaVEB, blaPER, and blaGES genes in β-lactam-resistant P. aeruginosa. We collected 100 non-duplicated clinical isolates of P. aeruginosa and identified them by standard tests. Using disk agar diffusion test, we detected the β-lactam-resistant isolates and extracted the DNAs of the isolates by alkaline lysis method. Then, the prevalence of blaVEB, blaPER and blaGES genes were detected by PCR method. The results were assessed by SPSS 21 software and Chi-square test. Out of 100 isolates, 43% were detected as resistant against at least one of the beta-lactams tested. Piperacillin-tazobactam was the most effective antibiotic, while 39% and 37% of the isolates were resistant to aztreonam and meropenem, respectively. A significant relationship was observed between the resistance to tested antibiotics and the presence of blaVEB, blaGES, and blaPER genes. Among 43 isolates that were resistant to at least one of the tested β-lactams, 93.02%, 83.72%, and 81.39% of them carried blaVEB, blaGES, and blaPER genes, respectively. According to this study and due to high prevalence of β-lactam resistance genes, it is better to check the level of antibiotic resistance and resistance genes for better management of patients with infection caused by this bacterium. Also, high prevalence of class A β-lactamases indicates the significant role of these enzymes in emerging resistance to beta-lactams.

    Citation: Saboura Haghighi, Hamid Reza Goli. High prevalence of blaVEB, blaGES and blaPER genes in beta-lactam resistant clinical isolates of Pseudomonas aeruginosa[J]. AIMS Microbiology, 2022, 8(2): 153-166. doi: 10.3934/microbiol.2022013

    Related Papers:

  • The increased prevalence of β-lactamase is one of the main factors in resistance to β-lactams in Pseudomonas aeruginosa. This study aimed to investigate the prevalence of blaVEB, blaPER, and blaGES genes in β-lactam-resistant P. aeruginosa. We collected 100 non-duplicated clinical isolates of P. aeruginosa and identified them by standard tests. Using disk agar diffusion test, we detected the β-lactam-resistant isolates and extracted the DNAs of the isolates by alkaline lysis method. Then, the prevalence of blaVEB, blaPER and blaGES genes were detected by PCR method. The results were assessed by SPSS 21 software and Chi-square test. Out of 100 isolates, 43% were detected as resistant against at least one of the beta-lactams tested. Piperacillin-tazobactam was the most effective antibiotic, while 39% and 37% of the isolates were resistant to aztreonam and meropenem, respectively. A significant relationship was observed between the resistance to tested antibiotics and the presence of blaVEB, blaGES, and blaPER genes. Among 43 isolates that were resistant to at least one of the tested β-lactams, 93.02%, 83.72%, and 81.39% of them carried blaVEB, blaGES, and blaPER genes, respectively. According to this study and due to high prevalence of β-lactam resistance genes, it is better to check the level of antibiotic resistance and resistance genes for better management of patients with infection caused by this bacterium. Also, high prevalence of class A β-lactamases indicates the significant role of these enzymes in emerging resistance to beta-lactams.


    Abbreviations

    MDR

    Multi-drug Resistant

    D-Ala-D-Ala

    D-Alanine-D-Alanine

    β-lactams

    Beta-lactams

    ESBL

    Extended-spectrum Beta-lactamase

    OXA

    Oxacillinase

    MIC

    Minimum Inhibitory Concentration

    TSB

    Trypticase Soy Broth

    CLSI

    Clinical and Laboratory Standards Institute

    ATCC

    American Type Culture Collection

    SDS

    Sodium Dodecyl Sulfate

    OD

    Optical Density

    PCR

    Polymerase Chain Reaction

    ICU

    Intensive Care Unit

    CCU

    Cardiac Care Unit

    XDR

    Extensively Drug Resistant

    加载中

    Acknowledgments



    We thank the laboratory staff of Zare, Razi, Bu-Ali Sina, Fatemeh Zahra, and Imam Khomeini hospitals for providing patients information and the collection of the clinical isolates.

    Conflicts of interest



    The authors declare no conflict of interest.

    Authors' contributions



    Hamid R. Goli conceptualized and designed the study protocol development, acquired and analyzed the data. Saboura Haghighi acquired the data, performed all microbiological and molecular laboratory work and drafted the manuscript. All authors revised and approved the final version of the manuscript.

    Data Availability



    All data generated or analyzed during this study are included in this published article.

    Funding



    This study is a report of a database from an MSc student thesis registered and carried out in Sana Institute of Higher Education, Sari, Iran, but not funded by any organization.

    [1] Potron A, Poirel L, Nordmann P (2015) Emerging broad-spectrum resistance in Pseudomonas aeruginosa and Acinetobacter baumannii: mechanisms and epidemiology. Int J Antimicrob Agent 45: 568-585. https://doi.org/10.1016/j.ijantimicag.2015.03.001
    [2] Ahmadian L, Haghshenas MR, Mirzaei B, et al. (2020) Distribution and molecular characterization of resistance gene cassettes containing class 1 integrons in multi-drug resistant (MDR) clinical isolates of Pseudomonas aeruginosa. Infect Drug Resist 13: 2773. https://doi.org/10.2147/IDR.S263759
    [3] Klockgether J, Cramer N, Wiehlmann L, et al. (2011) Pseudomonas aeruginosa genomic structure and diversity. Front Microbiol 2: 150. https://doi.org/10.3389/fmicb.2011.00150
    [4] Driscoll JA, Brody SL, Kollef MH (2007) The epidemiology, pathogenesis and treatment of Pseudomonas aeruginosa infections. Drugs 67: 351-368. https://doi.org/10.2165/00003495-200767030-00003
    [5] Lyczak JB, Cannon CL, Pier GB (2000) Establishment of Pseudomonas aeruginosa infection: lessons from a versatile opportunist. Microb Infect 2: 1051-1060. https://doi.org/10.1016/S1286-4579(00)01259-4
    [6] Tacconelli E, Magrini N, Kahlmeter G, et al. (2017) Global priority list of antibiotic-resistant bacteria to guide research, discovery, and development of new antibiotics. World Health Organiz 27: 318-327. Available from: https://www.aidsdatahub.org/resource/who-global-priority-list-antibiotic-resistant-bacteria
    [7] Pang Z, Raudonis R, Glick BR, et al. (2019) Antibiotic resistance in Pseudomonas aeruginosa: mechanisms and alternative therapeutic strategies. Biotech Adv 37: 177-192. https://doi.org/10.1016/j.biotechadv.2018.11.013
    [8] Thakuria B, Lahon K (2013) The beta lactam antibiotics as an empirical therapy in a developing country: an update on their current status and recommendations to counter the resistance against them. J Clin Diagn Res JCDR 7: 1207. https://doi.org/10.7860/JCDR/2013/5239.3052
    [9] Ibrahim ME, Abbas M, Al-Shahrai AM, et al. (2019) Phenotypic characterization and antibiotic resistance patterns of extended-spectrum β-Lactamase-and AmpC β-lactamase-producing Gram-negative bacteria in a referral hospital, Saudi Arabia. Canadian J Infect Dis Med Microbiol 2019. https://doi.org/10.1155/2019/6054694
    [10] Nasser M, Gayen S, Kharat AS (2020) Prevalence of β-lactamase and antibiotic-resistant Pseudomonas aeruginosa in the Arab region. J Glob Antimicrob Resist 22: 152-160. https://doi.org/10.1016/j.jgar.2020.01.011
    [11] Matlashewski G, Berghuis A, Sheppard D, et al. Handbook of Antimicrobial Resistance: Springer (2017). ISBN: 978-1-4939-0694-9
    [12] Ambler RP (1980) The structure of β-lactamases. Philos Trans R Soc Lond B Biol Sci 289: 321-331. https://doi.org/10.1098/rstb.1980.0049
    [13] Papp-Wallace KM, Becka SA, Taracila MA, et al. (2016) Exposing a β-lactamase “twist”: the mechanistic basis for the high level of ceftazidime resistance in the C69F variant of the Burkholderia pseudomallei PenI β-lactamase. Antimicrob Agents chemother 60: 777-788. https://doi.org/10.1128/AAC.02073-15
    [14] Rossolini G, Mantengoli E (2005) Treatment and control of severe infections caused by multiresistant Pseudomonas aeruginosa. Clin Microbiol Infect 11: 17-32. https://doi.org/10.1111/j.1469-0691.2005.01161.x
    [15] Bauernfeind A, Stemplinger I, Jungwirth R, et al. (1996) Characterization of beta-lactamase gene blaPER-2, which encodes an extended-spectrum class A beta-lactamase. Antimicrob Agents chemother 40: 616-620. https://doi.org/10.1128/AAC.40.3.616
    [16] Ranellou K, Kadlec K, Poulou A, et al. (2012) Detection of Pseudomonas aeruginosa isolates of the international clonal complex 11 carrying the blaPER-1 extended-spectrum β-lactamase gene in Greece. J Antimicrob Chemother 67: 357-361. https://doi.org/10.1093/jac/dkr471
    [17] Mushtaq S, Warner M, Livermore DM (2010) In vitro activity of ceftazidime+ NXL104 against Pseudomonas aeruginosa and other non-fermenters. J Antimicrob Chemother 65: 2376-2381. https://doi.org/10.1093/jac/dkq306
    [18] Ortiz de la Rosa JM, Nordmann P, Poirel L (2019) ESBLs and resistance to ceftazidime/avibactam and ceftolozane/tazobactam combinations in Escherichia coli and Pseudomonas aeruginosa. J Antimicrob Chemother 74: 1934-1939. https://doi.org/10.1093/jac/dkz149
    [19] Castanheira M, Simner PJ, Bradford PA (2021) Extended-spectrum β-lactamases: an update on their characteristics, epidemiology and detection. JAC-Antimicrob Resist 3: dlab092. https://doi.org/10.1093/jacamr/dlab092. https://doi.org/10.1093/jacamr/dlab092
    [20] Sahm DF, Weissfeld A, Trevino E (2002) Baily and Scott's diagnostic microbiology. Mosby, St Louis . ISBN: 9780323681056
    [21] Wayne P (2020) Performance standards for antimicrobial susceptibility testing; 29th informational supplement. CLSI document M100-S30. Maryland, USA: Clinical and Laboratory Standards Institute. ISBN: 978-168440-067-6
    [22] Šipošová NŠ, Liptáková V, Kvasnová S, et al. (2017) Genetic diversity of Acinetobacter spp. adapted to heavy metal polluted environments. Nova Biotech et Chim 16: 42-47. https://doi.org/10.1515/nbec-2017-0006
    [23] Jiang X, Zhang Z, Li M, et al. (2006) Detection of extended-spectrum β-lactamases in clinical isolates of Pseudomonas aeruginosa. Antimicrob Agents Chemother 50: 2990-2995. https://doi.org/10.1128/AAC.01511-05
    [24] Elhariri M, Hamza D, Elhelw R, et al. (2017) Extended-spectrum beta-lactamase-producing Pseudomonas aeruginosa in camel in Egypt: potential human hazard. Ann Clin Microbiol Antimicrob 16: 1-6. https://doi.org/10.1186/s12941-017-0197-x
    [25] Dehbashi S, Tahmasebi H, Alikhani MY, et al. (2020) Distribution of Class B and Class A β-lactamases in clinical strains of Pseudomonas aeruginosa: comparison of phenotypic methods and high-resolution melting analysis (HRMA) assay. Infect Drug Resist 13: 2037. https://doi.org/10.2147/IDR.S255292
    [26] Alikhani MY, Tabar ZK, Mihani F, et al. (2014) Antimicrobial resistance patterns and prevalence of blaPER-1 and blaVEB-1 genes among ESBL-producing Pseudomonas aeruginosa isolates in West of Iran. Jundishapur J Microbiol 7: e8888. https://doi.org/10.5812/jjm.8888
    [27] Endimiani A, Luzzaro F, Pini B, et al. (2006) Pseudomonas aeruginosa bloodstream infections: risk factors and treatment outcome related to expression of the PER-1 extended-spectrum beta-lactamase. BMC Infect Dis 6: 1-9. https://doi.org/10.1186/1471-2334-6-52
    [28] Rabiei MM, Asadi K, Shokouhi S, et al. (2020) Antipseudomonal β-Lactams Resistance in Iran. Int J Microbiol 2020: 8818315. https://doi.org/10.1155/2020/8818315
    [29] Bokaeian M, Zahedani SS, Bajgiran MS, et al. (2015) Frequency of PER, VEB, SHV, TEM and CTX-M genes in resistant strains of Pseudomonas aeruginosa producing extended spectrum β-lactamases. Jundishapur J Microbiol 8: e13783. https://doi.org/10.5812/jjm.13783
    [30] Philippon A, Slama P, Dény P, et al. (2016) A structure-based classification of class A β-lactamases, a broadly diverse family of enzymes. Clin Microbiol Rev 29: 29-57. https://doi.org/10.1128/CMR.00019-15
    [31] Delbrück H, Bogaerts P, Kupper MB, et al. (2012) Kinetic and crystallographic studies of extended-spectrum GES-11, GES-12, and GES-14 β-lactamases. Antimicrob Agents Chemother 56: 5618-5625. https://doi.org/10.1128/AAC.01272-12
    [32] Naas T, Poirel L, Nordmann P (2008) Minor extended-spectrum β-lactamases. Clin Microbiol Infect 14: 42-52. https://doi.org/10.1111/j.1469-0691.2007.01861.x
    [33] Shacheraghi F, Shakibaie MR, Noveiri H, et al. (2010) Molecular Identification of ESBL Genes blaGES-1, blaVEB-1, blaCTX-M, blaOXA-1, blaOXA-4, blaOXA-10 and blaPER-1 in Pseudomonas aeruginosa Strains Isolated from Burn Patients by PCR, RFLP and Sequencing Techniques. Int J Biol Life Sci 6: 138-142. https://doi.org/10.5281/zenodo.1327919
    [34] Shahcheraghi F, Nikbin VS, Feizabadi MM (2009) Prevalence of ESBLs genes among multidrug-resistant isolates of Pseudomonas aeruginosa isolated from patients in Tehran. Microb Drug Resist 15: 37-39. https://doi.org/10.1089/mdr.2009.0880
    [35] Zafer MM, Al-Agamy MH, El-Mahallawy HA, et al. (2014) Antimicrobial resistance pattern and their beta-lactamase encoding genes among Pseudomonas aeruginosa strains isolated from cancer patients. BioMed Res Int 2014: 101635. https://doi.org/10.1155/2014/101635
    [36] Adjei CB, Govinden U, Essack SY, et al. (2018) Molecular characterisation of multidrug-resistant Pseudomonas aeruginosa from a private hospital in Durban, South Africa. South African J Infect Dis 33: 38-41. https://doi.org/10.4102/sajid.v33i2.19
    [37] Sawa T, Kooguchi K, Moriyama K (2020) Molecular diversity of extended-spectrum β-lactamases and carbapenemases, and antimicrobial resistance. J Intensive Care 8: 1-13. https://doi.org/10.1186/s40560-020-0429-6
    [38] Croughs P, Klaassen C, van Rosmalen J, et al. (2018) Unexpected mechanisms of resistance in Dutch Pseudomonas aeruginosa isolates collected during 14 years of surveillance. Int J Antimicrob Agents 52: 407-410. https://doi.org/10.1016/j.ijantimicag.2018.05.009
    [39] Laudy AE, Róg P, Smolińska-Król K, et al. (2017) Prevalence of ESBL-producing Pseudomonas aeruginosa isolates in Warsaw, Poland, detected by various phenotypic and genotypic methods. PloS one 12: e0180121. https://doi.org/10.1371/journal.pone.0180121
    [40] Al-Agamy MH, Khalaf NG, Tawfick MM, et al. (2014) Molecular characterization of carbapenem-insensitive Acinetobacter baumannii in Egypt. Int J Infect Dis 22: 49-54. https://doi.org/10.1016/j.ijid.2013.12.004
    [41] Mirsalehian A, Feizabadi M, Nakhjavani FA, et al. (2010) Detection of VEB-1, OXA-10 and PER-1 genotypes in extended-spectrum β-lactamase-producing Pseudomonas aeruginosa strains isolated from burn patients. Burns 36: 70-74. https://doi.org/10.1016/j.burns.2009.01.015
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