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Marwa Raafat

Basic information

Name : Marwa Raafat
Title: Lecturer in Microbiology and Immunology
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Personal Info: Dr. Marwa Mahmoud Raafat, PhD ,Lecturer in Microbiology and Immunology; PhD in Medical Microbiology and Immunology, Assiut University; MSc in Microbiology, Meniya University; BSc in Pharmaceutical Sciences , Assiut University. View More...

Education

Certificate Major University Year
PhD Pharmaceutical Sciences in Medical Microbiology and Immunology Faculty of Pharmaceutical Sciences - Assiut University 2010
Masters Pharmaceutical Sciences in Microbiology Faculty of Pharmaceutical Sciences - El Minya University 2004
Bachelor Pharmaceutical Sciences " Faculty of Pharmaceutical Sciences - Assiut University 1998

Teaching Experience

Name of Organization Position From Date To Date
Assiut Univerisity Assiut Univesity, Faculty of Pharmacy 01/01/2006 01/01/2010
Minya University Minya University, Faculty of Pharmacy 01/01/2000 01/01/2005

Researches /Publications

Hindering of Cariogenic Streptococcus mutans Biofilm by Fatty Acid Array Derived from an Endophytic Arthrographis kalrae Strain. - 01/0

Marwa Mahmoud Raafat Abdel Fadiel Hassan

Abdel-Aziz MM, Emam TM

01/05/2020

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Production, characterization and bioinformatics analysis of l-asparaginase from a new Stenotrophomonas maltophilia EMCC2297 soil isolate. 2020 . - 01/0

Marwa Mahmoud Raafat Abdel Fadiel Hassan

Abdelrazek NA, Elkhatib WF, Aboulwafa MM.

01/01/2020

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Quorum quenching activity of Bacillus cereus isolate 30b confers antipathogenic effects in Pseudomonas aeruginosa - 01/0

Marwa Mahmoud Raafat Abdel Fadiel Hassan

01/06/2019

Background: Quorum quenching, the interference of a Quorum sensing (QS) system that contributes to the pathogenesis through triggering the production of various virulence determinants, is among the newly suggested antivirulence strategies. Purpose: This study aimed at screening of N-Acyl homoserine lactonase activity from local bacterial isolate, and investigating its effect on Pseudomonas aeruginosa (P. aeruginosa) virulence and biofilm formation. Materials and methods: Soil bacteria were screened for aiiA gene coding for lactonase enzyme by Polymerase Chain reaction and sequencing of aiiA gene homologs. Lactonase activity and spectrum were assessed in the cell-free lysate by well diffusion assay using Agrobacterium tumafaciens KYC55. A bacterial isolate showing the highest N-acyl-homoserine lactones degradation percentage was identified by gene amplification and sequencing of the 16S rRNA gene and its aiiA gene homolog. High performance liquid chromatography was used to confirm N-acyl-homoserine lactone degradation. The effect of cell-free lysate on the biofilm formation ability and cytotoxicity of P. aeruginosa PAO1 and P. aeruginosa clinical isolates from different clinical sources were assessed by static microtiter plate and viability assay, respectively Results: Lactonase gene and activity were identified in three Bacillus spp. isolates. They showed broad catalytic activities against tested N-acyl-homoserine lactones. However, The lactonase activity in the cell- free lysate of isolate 30b showed the highest significant degradation percentage on all tested signals; N-butanoyl-L-homoserine lactone (71%), N-hexanoyl-l-homoserine lactone (100%), N-decanoyl-homoserine lactone (100%), N-(3-oxohexanoyl)-L-homoserine lactone (37.5%), N-(oxodecanoyl)-L-homoserine lactone (100%), and N-(3-oxododecanoyl)-L-homoserine lactone (100%). Alignment of the amino acid sequences of AiiA protein of isolate 30b showed 96% identity with Bacillus cereus (B. cereus) homologous lactonases in the GenBank database, and the isolate was designated as B. cereus isolate 30b. Cell-free lysate of B. cereus isolate 30b reduced biofilm formation significantly in 93% of P. aeruginosa isolates. The highest mean percentage of reduction in the biofilm was 86%. Moreover, the viability percentage of human lung carcinoma A549 cells infected by P. aeruginosa and treated with cell-free lysate of B. cereus isolate 30b increased up to 15%. Conclusion: The results of this study highlight the potential of lactonases as a promising strategy to combat Pseudomonas aeruginosa virulence.

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Diverse origins of microbial L-asparaginases and their current miscellaneous applications - 01/0

Marwa Mahmoud Raafat Abdel Fadiel Hassan

Walid Faisal Elkhatib, Mohammad Aboulwafa

01/04/2019

L-asparaginase, also known as amidohydrolase, catalyzes the breakdown of asparagine into aspartic acid and ammonia. Due to its ability to inhibit the biosynthesis of protein lymphoblasts, it is used to treat acute lymphoblastic leukemia (ALL). It also has other applications in the food industry by preventing the formation of acrylamide. Different organisms including bacteria, fungi, actinomycetes, and plants produce L-asparaginase. This review highlights different applications of L-asparaginase in the industrial fields, the major sources of L-asparaginase, its immunological reactions and production techniques through the solid state (SSF) and submerged (SmF) fermentation as well as optimization of the production process.

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Experimental and bioinformatics study for production of l-asparaginase from Bacillus licheniformis: a promising enzyme for medical application - 01/0

Marwa Mahmoud Raafat Abdel Fadiel Hassan

Walid F. Elkhatib, Mohammad M. Aboulwafa

01/03/2019

A Bacillus licheniformis isolate with high L-asparaginase productivity was recovered upon screening two hundred soil samples. This isolate produces the two types of bacterial L-asparaginases, the intracellular type I and the extracellular type II. The catalytic activity of type II enzyme was much higher than that of type I and reached about 5.5 IU/ml/h. Bioinformatics analysis revealed that L-asparaginases of Bacillus licheniformis is clustered with those of Bacillus subtilis, Bacillus haloterans, Bacillus mojavensis and Bacillus tequilensis while it exhibits distant relatedness to L-asparaginases of other Bacillus subtilis species as well as to those of Bacillus amyloliquefaciens and Bacillus velezensis species. Upon comparison of Bacillus licheniformis L-asparaginase to those of the two FDA approved L-asparaginases of E. coli (marketed as Elspar) and Erwinia chrysanthemi (marketed as Erwinaze), it observed in a cluster distinct from- and with validly predicted antigenic regions number comparable to those of the two mentioned reference strains. It exhibited maximum activity at 40 °C, pH 8.6, 40 mM asparagine, 10 mM zinc sulphate and could withstand 500 mM NaCl and retain 70% of its activity at 70 °C for 30 min exposure time. Isolate enzyme productivity was improved by gamma irradiation and optimized by RSM experimental design (Box–Behnken central composite design). The optimum conditions for maximum L-asparaginase production by the improved mutant were 39.57 °C, 7.39 pH, 20.74 h, 196.40 rpm, 0.5% glucose, 0.1% ammonium chloride, and 10 mM magnesium sulphate. Taken together, Bacillus licheniformis L-asparaginase can be considered as a promising candidate for clinical application as antileukemic agent

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Synthesis, biological evaluation and molecular modeling study of new (1, 2, 4-triazole or 1, 3, 4-thiadiazole)-methylthio-derivatives of quinazolin-4 (3H)-one as DHFR inhibitors. - 01/0

Marwa Mahmoud Raafat Abdel Fadiel Hassan

Hanan H.Georgey,Shahenda M.El-Messery, Ghada S.Hassane

01/06/2017

A new series of 2-mercapto-quinazolin-4-one analogues was designed, synthesized and evaluated for their in vitro DHFR inhibition, antitumor and antimicrobial activity. Compound 17 proved to be the most active DHFR inhibitor with IC50 value of 0.01 μM, eight fold more active than methotrexate (MTX). Compounds 16 and 24 showed antitumor activity against human Caco2 colon and MCF-7 breast tumor cell lines with IC50 values of 25.4 and 9.5 μg/ml, respectively. Compounds 15, 20, 21 and 30 showed considerable activity against the Gram-positive bacteria Staphylococcus aureus while 24 and 30 proved active against Bacillus subtilis with a magnitude of potency comparable to the broad spectrum antibiotic Ciprofloxacin. Strong activity was observed for 13, 14, 19, 20 and 24 against Candida albicans and Aspergillus flavus. Compound 17 shared a similar molecular docking mode with MTX and made a critical hydrogen bond and arene-arene interactions via Ala9 and Phe34 amino acid residues, respectively.

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Synthesis, biological evaluation and molecular modeling study of new (1, 2, 4-triazole or 1, 3, 4-thiadiazole)-methylthio-derivatives of quinazolin-4 (3H)-one as DHFR inhibitors - 01/0

Marwa Mahmoud Raafat Abdel Fadiel Hassan

Hanan H. Georgey, Shahenda M. El-Messery, Ghada S. Hassan,

01/06/2016

A new series of 2-mercapto-quinazolin-4-one analogues was designed, synthesized and evaluated for their in vitro DHFR inhibition, antitumor and antimicrobial activity. Compound 17 proved to be the most active DHFR inhibitor with IC50 value of 0.01 μM, eight fold more active than methotrexate (MTX). Compounds 16 and 24 showed antitumor activity against human Caco2 colon and MCF-7 breast tumor cell lines with IC50 values of 25.4 and 9.5 μg/ml, respectively. Compounds 15, 20, 21 and 30 showed considerable activity against the Gram-positive bacteria Staphylococcus aureus while 24 and 30 proved active against Bacillus subtilis with a magnitude of potency comparable to the broad spectrum antibiotic Ciprofloxacin. Strong activity was observed for 13, 14, 19, 20 and 24 against Candida albicans and Aspergillus flavus. Compound 17 shared a similar molecular docking mode with MTX and made a critical hydrogen bond and arene-arene interactions via Ala9 and Phe34 amino acid residues, respectively.

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Awards

Award Donor Date
Award for best boaster presented in 22 nd annual Conference Faculty of Medcine, Assiut Universty 2004

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