Journals / Türk Mikrobiyoloji Cemiyeti Dergisi / 2021 / Cilt: 51 - Sayı: 1

Investigation of Phospholipase Activity in Candida albicans Strains Isolated From Blood and Oral Cavity Specimens

Kan ve Oral Kavite Örneklerinden Soyutlanan Candida albicans Suşlarının Fosfolipaz Aktivitelerinin Araştırılması§

Pages
50–60
Publication Date
2022-11-06
DOI
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While no significant difference was detected between PLB1 expression values of the groups (t=-0.307; p=0.760), PLB2 and PLC1 expressions were found to be significantly higher in blood (p=0.043) and oral cavity isolates (p

📌 3 Key Takeaways

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Objective & Hypothesis:Objective: The aim of the present study was to investigate and compare the phospholipase B1, B2, C1 and D1 activities in C.albicans strains isolated from blood cultures and oral cavity specimens.
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Key Findings & Data:Results: Twenty-six (86.7%) strains isolated from blood and 24 (80.0%) from oral cavities revealed phospholipase activity by plate method.
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Conclusion & Impact:While no significant difference was detected between PLB1 expression values of the groups (t=-0.307; p=0.760), PLB2 and PLC1 expressions were found to be significantly higher in blood (p=0.043) and oral cavity isolates (p
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Domain Parameters

Abstract

Objective: The aim of the present study was to investigate and compare the phospholipase B1, B2, C1 and D1 activities in C.albicans strains isolated from blood cultures and oral cavity specimens. Method: Phospholipase activity of the strains was examined by plate method and reverse transcriptase polymerase chain reaction (RT-PZT). Results: Twenty-six (86.7%) strains isolated from blood and 24 (80.0%) from oral cavities revealed phospholipase activity by plate method. No statistically significant difference (χ2=0.48; p=0.49) was observed between the groups. However statistical difference was determined between the mean Pz values (0.6138±0.9823; 0.6988±0.9910) (p=0.007). PLB1 expression was detected in all (100%), PLB2 in 29 (96.7%) and 30 (100.0%), PLC1 in 27 (90%) and 22 (73.3%), PLD1 in 27 (90.0%) and 21 (70.0%) of blood and oral strains, respectively. While no significant difference was detected between PLB1 expression values of the groups (t=-0.307; p=0.760), PLB2 and PLC1 expressions were found to be significantly higher in blood (p=0.043) and oral cavity isolates (p

Özet

Amaç: Bu çalışmada, kan ve oral kavite örneklerinden soyutlanan Candida albicans suşlarında, konak hücre membranlarındaki fosfolipitleri parçalayan fosfolipaz B1, B2, C1 ve D1 aktivitesinin incelenmesi ve grup farklılıklarının araştırılması amaçlandı. Yöntem: Suşların fosfolipaz aktivitesi, plak yöntemi ve ters transkriptaz polimeraz zincir tepkimesi (RT-PZT) ile araştırıldı. Bulgular: Plak yöntemi ile kan ve oral kavite suşlarının sırasıyla 26 (%86.7) ve 24’ünde (%80.0) fosfolipaz aktivitesi belirlendi. Grupların fosfolipaz olumluluk oranları karşılaştırıldığında, anlamlı bir fark gözlenmedi (χ2=0.48; p=0.49) ancak Pz ortalamaları (0.6138±0.9823, 0.6988±0.9910) arasında anlamlı bir fark saptandı (p=0.007). RT-PZT ile kan ve oral izolatların tümünde (%100) PLB1, sırasıyla 29 (%96.7) ve 30 (%100.0)’unda PLB2, 27 (%90.0)’si ve 22 (%73.3)’sinde PLC1, 27 (%90.0) ve 21 (%70.0)’inde ise PLD1 ekspresyonu belirlendi. PLB1 ekspresyonu açısından iki grup arasında anlamlı bir fark saptanmazken (t=-0.307; p=0.760), PLB2 ekspresyonu kan izolatlarında anlamlı derecede yüksek bulundu (p=0.043). PLC1 ekspresyon düzeyi oral suşlarda anlamlı derecede yüksek (p

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Cite This Article

GÜRBÜZ, E. D., DERELİ, M. D., TUNÇ, B. (2022). Investigation of Phospholipase Activity in Candida albicans Strains Isolated From Blood and Oral Cavity Specimens. Türk Mikrobiyoloji Cemiyeti Dergisi, Cilt: 51 - Sayı: 1, 50–60. https://ajindex.com/articles/635759

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References (12)

  1. Ying S, Chunyang L. Correlation between phospholipase of Candida albicans and resistance to fluconazole. Mycoses. 2012;55(1):50-5.
  2. Mavor AL, Thewes S, Hube B. Systemic fungal infections caused by Candida species: Epidemiology, infection process and virulance attributes. Curr Drug Targets. 2005;6(8):863-74.
  3. Martinez JP, Gil ML, Lopez-Ribot JL, Chaffin WL. Serologic response to cell wall mannoproteins and proteins of Candida albicans. Clin Microbiol Rev. 1998;11(1):121-41
  4. Niewerth M, Korting HC. Phospholipases of Candida albicans. Mycoses. 2001;44:361-7.
  5. Ghannoum MA. Potential role of phospholipases in virulence and fungal pathogenesis. Clin Microbiol Rev. 2000;13(1):122-43.
  6. Ibrahim AS, Mirbod F, Filler SG et al. Evidence implicating phospholipase as a virulence factor of Candida albicans. Infect Immun. 1995;63(5):1993-8.
  7. Ellepola ANB, Joseph BK, Khan ZU. The postantifungal effect and phospholipase production of oral Candida albicans from smokers, diabetics, asthmatics, denture wearers and healthy individuals following bries exposure to subtherapeutic concentrations of chlorhexidine gluconate. Mycoses. 2014;57(9):553-9.
  8. Samaranayeke LP, Raeside JM, MacFarlane TW. Factors affecting the phospholipase activity in Candida species in vitro. Sabouraudia. 1984;22(3):201-7
  9. Price MF, Wilkinson ID, Gentry LO. Plate method for detection of phospholipase activity in Candida albicans. Sabouraudia. 1982;20(1):7-14.
  10. Samaranayake YH, Dassanayake RS, Cheung BPK et al. Differential phosholipase gene expression by Candida albicans in artificial media and cultured human oral epithelium. APMIS. 2006;114(12):857-66.
  11. Samaranayake YH, Dassanayake RS, Jayatilake JA et al. Phospholipase B enzyme expression is not associated with other virulence attributes in Candida albicans isolates from patients with human immunodeficiency virüs infection. J Med Microbiol. 2005; 54:583-93.
  12. Henry KW, Nickels JT, Edlind TD. Upregulation of ERG genes in Candida species by azoles and other sterol biosynthesis inhibitors. Antimicrobial Agents and Chemotherapy. 2000;44(