The Characteristics Of The Pseudomonas aeruginosa And How To Prevention From Them.
DOI:
https://doi.org/10.36320/ajb/v14.i2.11714Keywords:
P. aeruginosa, Bacterial nosocomial infections, β-Lactamase, gram-negativeAbstract
The infections that causes by Pseudomonas aeruginosa is usually responsible for the nosocomial infections of the United States. Occurs in the each year approximality 51,000 cases of P. aeruginosa infections , and the persons the most risk of infection are those most exposer into equipment of hospital that has not well desinfection such as ventilation of mechanical and catheters.Some strains of P. aeruginosa that mutate or those that production of β-Lactamase enzymes that resistance into penicillins.The enzymes of β-Lactamase acts on the disruption into atomic structure of Carbapenems , Penicillins, Monobactams and Cephalosporins , and also the mechanisms that provides to resistance into penicillins such as efflux pumps of genetically encoded that acting as transmembrane proteins that help to secrete toxic materials. The mutations that influence to expression of gene for P. aeruginosa provide immune to support antimicrobials. So that results into decrease of specific genes that leads into production wide spectrum of β-Lactamase. The immune increase against penicillin and other antibiotics is important role play to the stay length of a patient's in hospital and rate of mortality.The conjugation of bacteria role play to an increase resistance for the antibiotics and some P. aeruginosa strains have become immune against all penicillins.The P. aeruginosa of illumination that leds into provides measures of preventative and steps that leads to fight of outbreaks nosocomial . These review aids into address mechanisms of resistance and discuss the preventative measures and its effectiveness that used today.
Downloads
References
Centers for Disease Control and Prevention (2014) Healthcare-associated Infections. [https://www.cdc.gov/hai/organisms/
pseudomonas.html] Retrieved on January 04, 2018.
Favero MS, Carson LA, Bond WW, Petersen NJ (1971) Pseudomonas aeruginosa: Growth in distilled water from hospitals. Science 173: 836-838. DOI: https://doi.org/10.1126/science.173.3999.836
Pollack M (2000) Pseudomonas aeruginosa. In: Mandell GL, Bennett JE, Dolin R, (eds). Principles and Practice of Infectious Diseases. (5th edn), Churchill Livingstone, New York, NY, USA. pp: 2310-2327.
Iglewski BH (1996) Pseudomonas. In: Baron S, (ed). Medical Microbiology. (4th edn). Galveston (TX): University of Texas Medical Branch at Galveston, Texas, USA.
Pollack M, Anderson SE Jr (1978) Toxicity of Pseudomonas aeruginosa exotoxin A for human macrophages. Infect Immun 19: 1092-1096. DOI: https://doi.org/10.1128/iai.19.3.1092-1096.1978
Beta Lactam Antibiotics (2011) Beta Lactam Antibiotics — Antimicrobial resistance learning site for veterinary students,
Michigan State Univeristy, USA.
Angus BL, Carey AM, Caron DA, Kropinski AM, Hancock RE (1982) Outer membrane permeability in Pseudomonas aeruginosa:
comparison of a wild-type with an antibiotic-supersusceptible mutant. Antimicrob Agents Chemother 21: 299-309. DOI: https://doi.org/10.1128/AAC.21.2.299
Masuda N, Sakagawa E, Ohya S, Gotoh N, Tsujimoto H, et al. (2000) Substrate specificities of MexAB-OprM, MexCD-OprJ, and MexXY-OprM efflux pumps in Pseudomonas aeruginosa. Antimicrob Agents Chemother 44: 3322-3327. DOI: https://doi.org/10.1128/AAC.44.12.3322-3327.2000
Debarati C, Anamika G, Debadatta DC, Anupam DT, Manabendra DC, et al. (2016) Premature termination of MexR leads to overexpression of MexAB-OprM efflux pump in Pseudomonas aeruginosa in a Tertiary Referral Hospital in India. PLoS ONE 11: E0149156. DOI: https://doi.org/10.1371/journal.pone.0149156
Lister PD, Wolter DJ, Hanson ND (2009) Antibacterial-resistant Pseudomonas aeruginosa: Clinical impact and complex regulation of
chromosomally encoded resistance mechanisms. Clin Microbiol Rev: 22: 582-610.
Srikumar R, Li XZ, Poole K (1997) Inner membrane efflux components are responsible for beta-lactam specificity of multidrug efflux pumps in Pseudomonas aeruginosa. J Bacteriol 179: 7875-7881. DOI: https://doi.org/10.1128/jb.179.24.7875-7881.1997
Okamoto K, Gotoh N, Nishino T (2002) Alterations of susceptibility of Pseudomonas aeruginosa by overproduction of multidrug efflux systems, MexAB-OprM, MexCD-OprJ, and MexXY/OprM to carbapenems: Substrate specificities of the efflux systems. J Infect Chemother 8: 371-373. DOI: https://doi.org/10.1007/s10156-002-0193-7
Aires JR, Köhler T, Nikaido H, Plésiat P (1999) Involvement of an active efflux system in the natural resistance of Pseudomonas aeruginosa to aminoglycosides. Antimicrob Agents Chemother 43: 2624–2628. DOI: https://doi.org/10.1128/AAC.43.11.2624
Chuanchuen R, Murata T, Gotoh N, Schweizer HP (2005) Substrate- dependent utilization of OprM or OpmH by the Pseudomonas
aeruginosa MexJK efflux pump. Antimicrob Agents Chemother 49: 2133–2136.
Stover CK, Pham XQ, Erwin AL, Mizoguchi SD, Warrener P (2000) Complete genome sequence of Pseudomonas aeruginosa PAO1, an DOI: https://doi.org/10.1038/35023079
opportunistic pathogen. Nature 406: 959-964.
Hoyle BD, Costerton JW (1991) Bacterial resistance to antibiotics: The role of biofilms. Prog. Drug Res 37: 91-105. DOI: https://doi.org/10.1007/978-3-0348-7139-6_2
Gurung J, Khyriem AB, Banik A, Lyngdoh WV, Choudhury B (2013) Association of biofilm production with multidrug resistance among clinical isolates of Acinetobacter baumannii and Pseudomonas aeruginosa from intensive care unit. Indian J Crit Care Med 17: 4214–218. DOI: https://doi.org/10.4103/0972-5229.118416
Trfipper DJ, Strominger JL (1965) Mechanism of action of penicillins: A proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc Natl Acad Sci USA 54: 1133–1141. DOI: https://doi.org/10.1073/pnas.54.4.1133
Spoering AL, Lewis K (2001) Biofilms and planktonic cells of Pseudomonas aeruginosa have similar resistance to killing by DOI: https://doi.org/10.1128/JB.183.23.6746-6751.2001
antimicrobials. J Bacteriol 183: 6746–6751.
Hendricks MR, Lashua LP, Fischer DK, Flitter BA, Eichinger KM, et al. (2016) Respiratory syncytial virus infection enhances Pseudomonas aeruginosa biofilm growth through dysregulation of nutritional immunity. Proc Natl Acad Sci U S A 113: 1642–1647. DOI: https://doi.org/10.1073/pnas.1516979113
Tielen P, Rosin N, Meyer AK, Dohnt K, Haddad I (2013) Regulatory and metabolic networks for the adaptation of Pseudomonas aeruginosa biofilms to urinary tract-like conditions. PLoS ONE 8: e71845. DOI: https://doi.org/10.1371/journal.pone.0071845
Lewis K (2001) Riddle of biofilm resistance. Antimicrob Agents Chemother 45: 999-1007. DOI: https://doi.org/10.1128/AAC.45.4.999-1007.2001
Lewis K (2005) Persister cells and the riddle of biofilm survival. Biochemistry (Mosc) 70: 267-274. DOI: https://doi.org/10.1007/s10541-005-0111-6
Brooun A, Liu S, Lewis K (2000) A dose-response study of antibiotic resistance in Pseudomonas aeruginosa biofilms. Antimicrob Agents Chemother 44: 640-646. DOI: https://doi.org/10.1128/AAC.44.3.640-646.2000
Zhang L, Fritsch M, Hammond L, Landreville R, Slatculescu C (2013) Identification of genes involved in Pseudomonas aeruginosa biofilm-specific resistance to antibiotics. PLoS ONE 8: e61625. DOI: https://doi.org/10.1371/journal.pone.0061625
Balasubramanian D, Schneper L, Merighi M, Smith R, Narasimhan G (2012) The regulatory repertoire of Pseudomonas aeruginosa AmpC ß-lactamase regulator ampr includes virulence genes. PLoS ONE 7: e34067. DOI: https://doi.org/10.1371/journal.pone.0034067
Shaikh S, Fatima J, Shakil S, Rizvi SM D, Kamal MA (2015) Antibiotic resistance and extended spectrum beta-lactamases: Types, DOI: https://doi.org/10.1016/j.sjbs.2014.08.002
epidemiology and treatment. Saudi J Biol Sci 22: 90-101. 30
Weldhagen GF, Poirel L, Nordmann P (2003) Ambler Class A extended-spectrum β-lactamases in Pseudomonas aeruginosa: Novel
developments and clinical impact. Antimicrob Agents Chemother 47: 2385–2392.
Neuhauser MM, Weinstein RA, Rydman R, Danziger LH, Karam G (2003) Antibiotic resistance among gram-negative bacilli in US DOI: https://doi.org/10.1001/jama.289.7.885
Intensive Care units: implications for fluoroquinolone use. JAMA 289: 85–888.
Lee M, Hesek D, Suvorov M, Lee W, Vakulenko S (2003) A mechanism-based inhibitor targeting the DD-transpeptidase activity of bacterial penicillin-binding proteins. J Am Chem Soc 125: 16322-16326. DOI: https://doi.org/10.1021/ja038445l
Jovetic S, Zhu Y, Marcone GL, Marinelli F, Tramper J (2010) β-Lactam and glycopeptide antibiotics: First and last line of defense? Trends Biotechnol 28: 596-604. DOI: https://doi.org/10.1016/j.tibtech.2010.09.004
Bonnet R (2004) Growing group of extended-spectrum β-lactamases: DOI: https://doi.org/10.1128/AAC.48.1.1-14.2004
The CTX-M enzymes. Antimicrob Agents Chemother 48: 1-14.
Evans BA, Amyes SG (2014) OXA β-lactamases. Clin Microbiol Rev 27: 241-263. DOI: https://doi.org/10.1128/CMR.00117-13
Ambler RP, Coulson AF, Frère JM, Ghuysen JM, Joris B (1991) A standard numbering scheme for the class A beta-lactamases. DOI: https://doi.org/10.1042/bj2760269
Biochem J 276: 269-270.
Dale JW, Smith JT (1974) R-Factor-Mediated β-lactamases that hydrolyze oxacillin: Evidence for two distinct groups. J Bacteriol 119: 351-356. DOI: https://doi.org/10.1128/jb.119.2.351-356.1974
Bush K, Jacoby GA, Medeiros AA (1995) A functional classification scheme for beta-lactamases and its correlation with molecular DOI: https://doi.org/10.1128/AAC.39.6.1211
structure. Antimicrob Agents Chemother 39: 1211-1233.
Santillana E, Beceiro A, Bou G, Romero A (2007) Crystal structure of the carbapenemase OXA-24 reveals insights into the mechanism of carbapenem hydrolysis. Proc Natl Acad Sci U S A 104: 5354-5359. DOI: https://doi.org/10.1073/pnas.0607557104
Bradford PA (2001) Extended-spectrum β-lactamases in the 21st
Century: Characterization, epidemiology, and detection of this important resistance threat. Clin Microbiol Rev 14: 933–951. DOI: https://doi.org/10.1128/CMR.14.4.933-951.2001
George ME, Bush k (2001) New β-lactamases in gram-negative bacteria: Diversity and impact on the selection of antimicrobial
therapy. Clin Infect 32: 1085–1089.
Bush K, Jacoby GA (2010) Updated functional classification of β-lactamases. Antimicrob Agents Chemother 54: 969-976. DOI: https://doi.org/10.1128/AAC.01009-09
Poirel L, Ronco E, Naas T, Nordmann P (1999) Extended-spectrum β-lactamase TEM-4 in Pseudomonas aeruginosa. Clin Microbiol Infect 5: 651–652. DOI: https://doi.org/10.1111/j.1469-0691.1999.tb00425.x
Mugnier P, Dubrous P, Casin I, Arlet G, Collatz E (1996) A TEM-derived extended-spectrum beta-lactamase in Pseudomonas aeruginosa. Antimicrob Agents Chemother 40: 2488-2493. DOI: https://doi.org/10.1128/AAC.40.11.2488
Bauernfeind A, Stemplinger I, Jungwirth R, Mangold P, Amann S (1996) Characterization of beta-lactamase gene blaPER-2, which
encodes an extended-spectrum class A beta-lactamase. Antimicrob Agents Chemother 40: 616–620.
Vahaboglu H, Oztürk R, Aygün G, Coşkunkan F, Yaman A (1997) Widespread detection of PER-1-type extended-spectrum beta-
lactamases among nosocomial Acinetobacter and Pseudomonas aeruginosa isolates in Turkey: A nationwide multicenter study.
Antimicrob Agents Chemother 41: 2265–2269.
Vahaboglu H, Oztürk R, Aygün G, Coşkunkan F, Yaman A (2005) Clavulanic acid inactivation of SHV-1 and the inhibitor-resistant
S130G SHV-1 β-lactamase. Insights into the mechanism of inhibition. J Biol Chem 280: 35528-35536.
Weldhagen GF, Poirel L, Nordmann P (2003) Ambler class A extended-spectrum β-lactamases in Pseudomonas aeruginosa: Novel
developments and clinical impact. Antimicrob Agents Chemother 47: 2385-2392.
De Champs C, Poirel L, Bonnet R, Sirot D, Chanal C, et al. (2002)Prospective survey of β-lactamases produced by ceftazidime-
resistant Pseudomonas aeruginosa isolated in a French Hospital in 2000. Antimicrob Agents Chemother 46: 3031-3034.
Empel J, Filczak K, Mrówka A, Hryniewicz W, Livermore DM, et al.(2007) Outbreak of Pseudomonas aeruginosa infections with PER-
extended-spectrum β-lactamase in Warsaw, Poland: Further Vol.2 No.2:18 evidence for an international clonal complex . J Clin Microbiol 45: 2829–2834. DOI: https://doi.org/10.1128/JCM.00997-07
Szabó D, Szentandrássy J, Juhász Z, Katona K, Nagy K (2008) Imported PER-1 producing Pseudomonas aeruginosa, PER-1 producing Acinetobacter baumanii and VIM-2-producing Pseudomonas aeruginosa strains in Hungary. Ann Clin Microbiol Antimicrob 7: 12. DOI: https://doi.org/10.1186/1476-0711-7-12
Pagani L, Mantengoli E, Migliavacca R, Nucleo E, Pollini S (2004) Multifocal detection of multidrug-resistant Pseudomonas aeruginosa
producing the PER-1 Extended-Spectrum β-lactamase in Northern Italy. J Clin Microbiol 42: 2523-2529. DOI: https://doi.org/10.1128/JCM.42.6.2523-2529.2004
Zafer MM, Al-Agamy MH, El-Mahallawy HA, Amin MA, Ashour MS (2014) Antimicrobial resistance pattern and their beta-lactamase DOI: https://doi.org/10.1155/2014/101635
encoding genes among Pseudomonas aeruginosa strains isolated from cancer patients. Biomed Res Int pp: 101635
Eraç B, Hoşgör-Limoncu M, Ermertcan Ş, Taşlı H, Aydemir Ş (2013) Prevalence of blaPER-1 and Integrons in ceftazidime-resistant gram-negative bacteria at a University Hospital in Turkey. Jpn J Infect Dis 66: 146-148. DOI: https://doi.org/10.7883/yoken.66.146
Danel F, Hall LM, Gur D, Akalin HE, Livermore DM (1995) Transferable production of PER-1 beta-lactamase in Pseudomonas aeruginosa. J Antimicrob Chemother 35: 281-294. DOI: https://doi.org/10.1093/jac/35.2.281
Bae IK, Jang SJ, Kim J, Jeong SH, Cho B (2011) Interspecies dissemination of the bla gene encoding PER-1 extended-spectrum
β-lactamase . Antimicrob Agents Chemother 55: 1305-1307.
Liakopoulos A, Mevius D, Ceccarelli D (2016) A review of SHV extended-spectrum β-lactamases: Neglected yet ubiquitous. Front DOI: https://doi.org/10.3389/fmicb.2016.01374
Microbiol 7: 1374.
Chen Z, Niu H, Chen G, Li M, Li M, et al. (2015) Prevalence of ESBLs-producing Pseudomonas aeruginosa isolates from different wards in a Chinese teaching hospital. Int J Clin Exp Med 8: 19400–19405.
Poirel L, Lebessi E, Castro M, Fèvre C, Foustoukou M, et al. (2004). Nosocomial outbreak of extended-spectrum β-lactamase SHV-5-
producing isolates of Pseudomonas aeruginosa in Athens, Greece. Antimicrobial Agents and Chemotherapy, 48: 2277–2279.
Izaki K, Matsuhashi M, Strominger JL (1966) Glycopeptide transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive DOI: https://doi.org/10.1016/0076-6879(66)08088-1
enzymatic reactions. Proc Natl Acad Sci U S A: 55: 656-663.
Sykes RB, Morrb A (1975) Resistance of Pseudomonas aeruginosa to antimicrobiol drugs. Prog Med Chem 12: 333-393. DOI: https://doi.org/10.1016/S0079-6468(08)70180-2
Yoshimura F, Nikaido H (1982) Permeability of Pseudomonas aeruginosa outer membrane to hydrophilic solutes. J Bacteriol 152: DOI: https://doi.org/10.1128/jb.152.2.636-642.1982
-642.
Nikaido H (1998) The role of outer membrane and efflux pumps in the resistance of gram-negative bacteria. Can we improve drug DOI: https://doi.org/10.1016/S1368-7646(98)80023-X
access? Drug Resistance Updates 1: 93-98.
Straatsma TP, Soares TA (2009) Characterization of the outer membrane protein OprF of Pseudomonas aeruginosa in a lipopolysaccharide membrane by computer simulation. Proteins, 74: 475-488. DOI: https://doi.org/10.1002/prot.22165
Li XZ, Plésiat P, Nikaido H (2015) The challenge of efflux-mediated antibiotic resistance in gram-negative bacteria. Clin Microbiol Rev DOI: https://doi.org/10.1128/CMR.00117-14
: 337–418.
Nikaido H (2003) Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67: 593-656. DOI: https://doi.org/10.1128/MMBR.67.4.593-656.2003
Quale J, Bratu S, Gupta J, Landman D (2006) Interplay of Efflux System, ampC, and oprD expression in carbapenem resistance
of Pseudomonas aeruginosa clinical isolates. Antimicrob Agents Chemother 50: 1633–1641.
Bell A, Bains M, Hancock RE (1991) Pseudomonas aeruginosa outer membrane protein OprH: expression from the cloned gene and function in EDTA and gentamicin resistance. J Bacteriol 173: 6657–6664. DOI: https://doi.org/10.1128/jb.173.21.6657-6664.1991
Magiorakos AP, Srinivasan A, Carey RB, Carmeli Y, Falagas ME, et al. (2012) Multidrug-resistant, extensively drug-resistant and pandrug-resistant bacteria: an international expert proposal for interim standard definitions for acquired resistance. Clin Microbiol Infect 18: 268-281. DOI: https://doi.org/10.1111/j.1469-0691.2011.03570.x
Saint S, Kowalski CP, Kaufman SR, Hofer TP, Kauffman CA (2008) Preventing hospital-acquired urinary tract infection in the United DOI: https://doi.org/10.1086/524662
States: A National Study. Clin Infect Dis 46: 243-250.
Schumm K, Lam TB (2008) Types of urethral catheters for management of short-term voiding problems in hospitalized adults: DOI: https://doi.org/10.1002/14651858.CD004013.pub3
A short version cochrane review. Neurourol Urodyn 27: 738–746.
Warren JW (2001) Catheter-associated urinary tract infections. Int J Antimicrob Agents 17: 299-303. DOI: https://doi.org/10.1016/S0924-8579(00)00359-9
Micek ST, Lloyd AE, Ritchie DJ, Reichley RM, Fraser VJ, et al. (2005) Pseudomonas aeruginosa bloodstream infection: Importance of appropriate initial antimicrobial treatment. Antimicrob Agents Chemother 49: 1306-1311. DOI: https://doi.org/10.1128/AAC.49.4.1306-1311.2005
Daniels KR, Frei CR (2013) The United States' progress toward eliminating catheter-related bloodstream infections: Incidence, mortality, and hospital length of stay from 1996 to 2008. Am J Infect Control 41: 118-121. DOI: https://doi.org/10.1016/j.ajic.2012.02.013
Lyczak JB, Cannon CL, Pier GB (2002) Lung infections associated with cystic fibrosis. Clin Microbiol Rev 15: 194-222. DOI: https://doi.org/10.1128/CMR.15.2.194-222.2002
Koenig SM, Truwit JD (2006) Ventilator-associated pneumonia: Diagnosis, treatment and prevention. Clin Microbiol Rev 19: 637-657. DOI: https://doi.org/10.1128/CMR.00051-05
Alp E, Voss A (2006) Ventilator associated pneumonia and infection control. Ann Clin Microbiol Antimicrob 5: 7. DOI: https://doi.org/10.1186/1476-0711-5-7
Kalanuria AA, Zai W, Mirski M (2014) Ventilator-associated pneumonia in the ICU. Crit Care 18: 208. DOI: https://doi.org/10.1186/cc13775
Metersky ML, Wang Y, Klompas M, Eckenrode S, Bakullari A (2016) Trend in Ventilator-Associated Pneumonia Rates Between 2005 and 2013. JAMA 316: 2427-2429. DOI: https://doi.org/10.1001/jama.2016.16226
Berriel-Cass D, Adkins FW, Jones P, Fakih MG (2006) Eliminating nosocomial infections at Ascension Health. Jt Comm J Qual Patient DOI: https://doi.org/10.1016/S1553-7250(06)32079-X
: 612-620.
Unahalekhaka A, Jamulitrat S, Chongsuvivatwong V, Ovretveit J (2007) Using a collaborative to reduce ventilator-associated pneumonia in Thailand. Jt Comm J Qual Patient Sa 33: 387-394. DOI: https://doi.org/10.1016/S1553-7250(07)33044-4
O'Grady NP, Murray PR, Ames N (2012) Preventing ventilator-associated pneumonia: Does the evidence support the practice? DOI: https://doi.org/10.1001/jama.2012.6445
JAMA 307: 2534-2539.
Timsit JF, Esaied W, Neuville M, Bouadma L, Mourvllier B (2017) Update on ventilator-associated pneumonia. F1000Res 6: 2061. DOI: https://doi.org/10.12688/f1000research.12222.1
Stone PW (2009) Economic burden of healthcare-associated infections: An American perspective. Expert Rev Pharmacoecon Outcomes Res 9: 417-422. DOI: https://doi.org/10.1586/erp.09.53
Recommendation of the Federal Environment Agency after Consultation with the Drinking Water Commission (2017) Recommendation for required studies on Pseudomonas aeruginosa, or risk assessment and measures for detection in drinking water.
Bundesgesundheitsblatt Gesundheitsforschung Gesundheitsschutz 60: 1180-1183.
Bédard E, Prévost M, Déziel E (2016) Pseudomonas aeruginosa in premise plumbing of large buildings. Microbiologyopen 5: 937-956. DOI: https://doi.org/10.1002/mbo3.391
Brook I (2011) Microbiology of sinusitis. Proc Am Thorac Soc 8: 90-100. DOI: https://doi.org/10.1513/pats.201006-038RN
Razek AAKA (2014) Computed tomography and magnetic resonance imaging of lesions at masticator space. Jpn J Radiol 32:
-137.
Razek AA, Sieza S, Maha B (2009) Assessment of nasal and paranasal sinus masses by diffusion-weighted MR imaging. J Neuroradiol 36: 206-211.
Razek AA (2010) Diffusion-weighted magnetic resonance imaging of head and neck. J Comput Assist Tomogr 34: 808-815. DOI: https://doi.org/10.1097/RCT.0b013e3181f01796
Razek AAKA .(2014). Computed tomography and magnetic resonance imaging of lesions at masticator space. Jpn J Radiol 32: DOI: https://doi.org/10.1007/s11604-014-0289-x
-137.
Razek AA, Sieza S, Maha B .(2009). Assessment of nasal and paranasal sinus masses by diffusion-weighted MR imaging. J Neuroradiol 36: 206-211. DOI: https://doi.org/10.1016/j.neurad.2009.06.001
Downloads
Published
How to Cite
Issue
Section
License
Copyright (c) 2022 Abdul Hussain, Abdulhasan Mshachal
This work is licensed under a Creative Commons Attribution 4.0 International License.
which allows users to copy, create extracts, abstracts, and new works from the Article, alter and revise the Article, and make commercial use of the Article (including reuse and/or resale of the Article by commercial entities), provided the user gives appropriate credit (with a link to the formal publication through the relevant DOI), provides a link to the license, indicates if changes were made and the licensor is not represented as endorsing the use made of the work.