American Journal of Microbiological Research

ISSN (Print): 2328-4129

ISSN (Online): 2328-4137

Editor-in-Chief: Apply for this position

Website: http://www.sciepub.com/journal/AJMR

   

Article

Effect of Trigona Honey to mRNA Expression of Interleukin-6 on Salmonella Typhi Induced of BALB/c Mice

1School of Nursing, Hasanuddin University, Makassar, Indonesia

2Department of Biochemistry, Hasanuddin University, Makassar, Indonesia

3Department of ENT, Hasanuddin University, Makassar, Indonesia

4Department of Epidemiology, Indonesia Timur University; Daya Regional Hospital-College of Health Science, Makassar, Indonesia

5Department of Microbiology, Faculty of Medicine, Tadulako University, Palu, Indonesia

6Molecular Biology and Immunology Laboratory, Faculty of Medicine, Hasanuddin University, Makassar, Indonesia


American Journal of Microbiological Research. 2016, 4(3), 77-80
doi: 10.12691/ajmr-4-3-2
Copyright © 2016 Science and Education Publishing

Cite this paper:
Yuliana Syam, Rosdiana Natsir, Sutji Pratiwi Rahardjo, Andi Nilawati Usman, Ressy Dwiyanti, Mochammad Hatta. Effect of Trigona Honey to mRNA Expression of Interleukin-6 on Salmonella Typhi Induced of BALB/c Mice. American Journal of Microbiological Research. 2016; 4(3):77-80. doi: 10.12691/ajmr-4-3-2.

Correspondence to: Mochammad  Hatta, Molecular Biology and Immunology Laboratory, Faculty of Medicine, Hasanuddin University, Makassar, Indonesia. Email: Hattaram@indosat.net.id

Abstract

Weak inflammatory response after Salmonella infection can cause persistent infection and facilitate the long survival of pathogens. Honey can induce key immunomodulators such as TNF-α, interleukin-6 (IL-6) and IL-1, that it can be used in the treatment of bacterial infectious diseases caused by Salmonella typhi. The purpose of this study is to determine the effect of honey on the mRNA expression of IL-6 in Salmonella enterica Typhi induced of BABL/c mice. The study used experimental pretest-posttest control design. Honey treatment was given for 7 days commencing after the induction of Salmonella bacteria. 20 BABL/c males mice whose weight 25-29 grams, were divided into four groups where 5 mice per group within; the negative control group was given regular feed without bacteria induction, the positive control group was given regular feed with bacteria induction, 0.27 ml/kg-weight honey group and 0.27 ml/kg-weight of Propolis honey group. Blood samples for examination of mRNA expression was examined three times that prior to the induction, 24 hours after induction and 72 hours after induction of Salmonella. The results showed that 0.27 ml/kg-weight of Propolis honey group showed the highest mRNA expression (p = 0.000) for both after 24 hours after induction of Salmonella typhi (p = 0.000) and 72 hours after induction of Salmonella typhi (p = 0.000). We conclude that there was effect of honey on the mRNA IL-6 expression in Salmonella typhi induced of BALB/c mice.

Keywords

References

[1]  Kassim, M., et al., Ellagic acid, phenolic acids, and flavonoids in Malaysian honey extracts demonstrate in vitro anti-inflammatory activity. Nutr Res, 2010. 30(9): p. 650-9.
 
[2]  Kassim, M., et al., Gelam honey inhibits lipopolysaccharide-induced endotoxemia in rats through the induction of heme oxygenase-1 and the inhibition of cytokines, nitric oxide, and high-mobility group protein B1. Fitoterapia, 2012. 83(6): p. 1054-9.
 
[3]  Tonks, A.J., et al., Honey stimulates inflammatory cytokine production from monocytes. Cytokine, 2003. 21(5): p. 242-7.
 
[4]  Al-Jabri, A.A., Honey, milk and antibiotics. African Journal of Biotechnology, 2005. 4(13): p. 1580-1587.
 
[5]  Molan, P.C., Potential of honey in the treatment of wounds and burns. Am J Clin Dermatol, 2001. 2(1): p. 13-9.
 
Show More References
[6]  Hannan , J., Saleem . Effect of different doses of Manuka honey in experimentally induced mouse typhoid. j pharm sci, 2015. 28.(3): p. 891-902.
 
[7]  Donya Nikaein, A.R.K., Zahra Moosavi, Hojjatollah Shokri, Ahmad Erfanmanesh, and H.G.-C.a.H. Bagheri, Effect of honey as an immunomodulator against invasive aspergillosis in BALB/c mice. Journal of Apicultural Research 2014. 53(1): p. 84-90.
 
[8]  Kim YS, Jung DH, Lee IS, Choi SJ, Yu SY, Ku SK, Kim MH, Kim J S. 2013. Effects of Allium victorialis leaf extracts and its single compounds on aldose reductase, advanced glycation end products and TGF-beta1 expression in mesangial cells. BMC Complement Altern Med, 13, 251.
 
[9]  Ayundria MRI. 2014. Bioactivity of Proplis to the CD4 + and CD8+ T cells Producing IFN-γ Cytokines in BALB /C Mice. Jurnal Biotropika, 2.
 
Show Less References

Article

Fluoroquinolones as Urease Inhibitors: Anti-Proteus mirabilis Activity and Molecular Docking Studies

1Departement of Medicinal Chemistry, Faculty of Pharmacy, Minia University, Minia, Egypt

2Departement of Microbiology and Immunology, Faculty of Pharmacy, Minia University, Minia, Egypt


American Journal of Microbiological Research. 2016, 4(3), 81-84
doi: 10.12691/ajmr-4-3-3
Copyright © 2016 Science and Education Publishing

Cite this paper:
Mohammed A. A. Abdullah, Rehab M. Abd El-Baky, Heba A. Hassan, El-Shimaa M. N. Abdelhafez, Gamal El-Din A. Abuo-Rahma. Fluoroquinolones as Urease Inhibitors: Anti-Proteus mirabilis Activity and Molecular Docking Studies. American Journal of Microbiological Research. 2016; 4(3):81-84. doi: 10.12691/ajmr-4-3-3.

Correspondence to: Rehab  M. Abd El-Baky, Departement of Microbiology and Immunology, Faculty of Pharmacy, Minia University, Minia, Egypt. Email: dr_rehab010@yahoo.com, rehab.mahmoud@mu.edu.eg

Abstract

The anti-Proteus mirabilis activity and MIC of levofloxacin and ciprofloxacin were investigated in comparison with the known urease inhibitor acetohydroxamic acid using Well Diffusion method. Also, their inhibitory effect on urease was determined by measuring ammonia production as an indicator of urease activity using the indophenol method as described by Weatherburn. AHA showed a weak anti-Proteus mirabilis activity the (MIC = 614.8 µM) than the two tested fluoroquinolones (MIC for levofloxacin = 3.2 µM and for ciprofloxacin = 15.62 µM). The tested fluoroquinolones experienced excellent urease inhibitory activity IC50 for levofloxacin = 2.9 µM and for ciprofloxacin = 3.5 µM). However, the results were supported by molecular docking studies to gain insights into the binding conformations as well as the inhibition mode of urease and showed coordination binding with the two Ni ion in the active site which are essential for urea breakdown.

Keywords

References

[1]  Mobley H.L., Hausinger R.P., Microbial ureases: significance, regulation, and molecular characterization, Microbiol. Rev. 53(1) (1989) 85-108.
 
[2]  Preininger C., Wolfbeis O.S., Disposable cuvette test with integrated sensor layer for enzymatic determination of heavy metals, Biosensors and Bioelectronics. 11 (1996) 981-990.
 
[3]  Mobley, H. L., Michael D. Island, and Robert P. Hausinger. “Molecular biology of microbial ureases.” Microbiological reviews59.3 (1995): 451-480.
 
[4]  Bairoch A., The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000, Nucleic Acids Research. 28 (2000) 45-48.
 
[5]  Muri E., Mishra H., Stein S., Williamson J., Molecular Modeling, Synthesis and Biological Evaluation of Heterocyclic Hydroxamic Acids Designed as Helicobacter pylori Urease Inhibitors, Letters in Drug Design & Discovery. 1 (2004) 30-34.
 
Show More References
[6]  Kuehler T.C., Fryklund J., Bergman N., Weilitz J., Lee A., Larsson H., Structure-Activity Relationship of Omeprazole and Analogs as Helicobacter pylori Urease Inhibitors, Journal of Medicinal Chemistry. 38 (1995) 4906-4916.
 
[7]  Faraci W.S. , Yang B.V., O’Rourke D., Spencer R.W., Inhibition of Helicobacter pylori Urease by Phenyl Phosphorodiamidates: Mechanism of Action, Bioorganic & Medicinal Chemistry. 3 (1995) 605-610.
 
[8]  Fishbein N., Carbone P.P., Urease Catalysis: II. Inhibition of the enzyme by hydroxyurea, hydroxylamine, and acetohydroxamic acid, Journal of Biological Chemistry. 240 (1965) 2407-2414.
 
[9]  Amtul Z., Atta-ur-Rahman B.S.P., Siddiqui R., Choudhary M., Chemistry and Mechanism of Urease Inhibition, Current Medicinal Chemistry. 9 (2002) 1323-1348.
 
[10]  Kumaki K., Tomioka S., Kobashi K., Hase J., Structure-Activity Correlations between Hydroxamic Acids and Their Inhibitory Powers on Urease Activity. I. A Quantitative Approach to the Effect of Hydrophobic Character of Acyl Residue, Chemical & pharmaceutical bulletin. 20 (1972) 1599-1606.
 
[11]  Williams J.J., Rodman J.S., Peterson C.M., A Randomized Double-Blind Study of Acetohydroxamic Acid in Struvite Nephrolithiasis, New England Journal of Medicine. 311 (1984) 760-764.
 
[12]  Kosikowska P., Berlicki L., Urease inhibitors as potential drugs for gastric and urinary tract infections: a patent review Expert Opin. Ther. Patents (2011) 21(6):945-957.
 
[13]  Abraham D.J.: Quinolone, in Burger’s Medicinal Chemistry Drug Discovery, p. 582-587, John Wiley and Sons, Hoboken, New Jersey 2003.
 
[14]  Ramadan M.A., Tawfik A.F., El-Kersh T.A., Shibl A.M., In vitro activity of subinhibitory concentrations of quinolones on urea-splitting bacteria: effect on urease activity and on cell surface hydrophobicity, Journal of Infectious Diseases. 171 (1995) 483-486.
 
[15]  Benson H.C., Benson’s microbiological applications: laboratory manual in general microbiology, short version, 11th ed. p. 168., McGraw-Hill Higher Education; McGraw-Hill, New York; London, 2010.
 
[16]  Sherertz R.J., Raad I.I., Belani A., Koo L.C., Rand K.H., Pickett D.L., et al., Three-year experience with sonicated vascular catheter cultures in a clinical microbiology laboratory., 28(1), 76-82.
 
[17]  Prywer J., Torzewska A., Płociński T., Unique surface and internal structure of struvite crystals formed by Proteus mirabilis, Urological Research. 40 (2012) 699-707.
 
[18]  Bibby J.M., Hukins D.W.L., Measurement of pH to quantify urease activity, Journal of Biochemical and Biophysical Methods. 25 (1992) 231-236.
 
[19]  Goldie, J., et al. “Optimization of a medium for the rapid urease test for detection of Campylobacter pylori in gastric antral biopsies.” Journal of clinical microbiology 27.9 (1989): 2080-2082.
 
[20]  Tanaka T., Kawase M., Tani S., Urease inhibitory activity of simple α, β-unsaturated ketones, Life Sciences. 73 (2003) 2985-2990.
 
[21]  Golbabaei S., Bazl R., Golestanian S., Nabati F., Omrany Z.B., Yousefi B., et al., Urease inhibitory activities of β-boswellic acid derivatives, DARU Journal of Pharmaceutical Sciences. 21(2) (2013) 2.
 
[22]  Akhtar T., Khan M.A., Iqbal J., Jones P.G., Hameed S., A Facile One-Pot Synthesis of 2-Arylamino-5-Aryloxylalkyl-1,3,4-Oxadiazoles and Their Urease Inhibition Studies, Chemical Biology & Drug Design. 84 (2014) 92-98.
 
[23]  Weatherburn M.W., Phenol-hypochlorite reaction for determination of ammonia, Analytical Chemistry. 39 (8) (1967) 971-974.
 
Show Less References

Article

Isolation and Molecular Identification of Fungi in Stored Maize (Zea mays L) and Groundnuts (Arachis hypogaea L) in Ngaoundere, Cameroon

1ENSAI, University of Ngaoundere, P.O. box 454, Ngaoundere, Cameroon

2IUT, University of Ngaoundere, P.O. box 454, Ngaoundere, Cameroon

3Faculty of Science, University of Douala, P.O. box 24157, Douala, Cameroon

4Environmental Technology Division, CSIR-NIIST, 695019 Thiruvananthapuram, India

5Faculty of Science, University of Ngaoundere, P.O. box 454, Ngaoundere, Cameroon


American Journal of Microbiological Research. 2016, 4(3), 85-89
doi: 10.12691/ajmr-4-3-4
Copyright © 2016 Science and Education Publishing

Cite this paper:
Agwanande Ambindei Wilson, Tatsadjieu Ngoune Leopold, Jazet Dongmo Pierre Michel, Priya P, Anie Mariya, Manilal V. B., Krishnakumar B, Amvam Zollo Paul Henri. Isolation and Molecular Identification of Fungi in Stored Maize (Zea mays L) and Groundnuts (Arachis hypogaea L) in Ngaoundere, Cameroon. American Journal of Microbiological Research. 2016; 4(3):85-89. doi: 10.12691/ajmr-4-3-4.

Correspondence to: Agwanande  Ambindei Wilson, ENSAI, University of Ngaoundere, P.O. box 454, Ngaoundere, Cameroon. Email: agwanande@gmail.com

Abstract

A knowledge of the specific fungi responsible for food spoilage in an ecological zone is paramount for proper preservation. The main objective of this study was to isolate and identify at the molecular level the different fungal species from contaminated stored maize and groundnuts. Contaminated grains from local markets in Ngaoundere, Cameroon were used for the study. Their average percentage water content was 16.75±0.27 and 11.24±0.31 for maize and groundnuts respectively. Nine fungal strains were isolated and identified through 18S rDNA sequencing. It was found that Rhizopus oryzae, Aspergillus flavus, Aspergillus oryzae and Cunninghamella polymorpha were common in both maize and groundnuts. Aspergillus tamari, Talaromyces purpureogenus and Penicillium citrinum were present only in maize, while Aspergillus parasiticus and Rhizopus stolonifer were identified only from groundnuts. The novel information presented in this study will help to formulate measures to control the fungal contamination of stored maize and groundnut.

Keywords

References

[1]  Pitt, J. I., and Hocking, A. D., Fungi and Food Spoilage, 3rd edition, Springer Science plus Business Media, LLC, 233 Spring Street, New York, NY 10013, USA, 524 pp. (2009).
 
[2]  Meyer A., Deiana J. and Bernard A. Cour de microbiologie générale. Doin. France, unpublished data. (2004).
 
[3]  FAO, Safety evaluation of certain mycotoxins in food. Prepared by the 56th meeting of the joint FAO/WHO Expert Committee on Food Additives (JECFA). FAO food and nutrition paper, Rome, FAO 74. 1-25 (2001).
 
[4]  Golob, P., Kutukwa, N., Devereau, A., Bartosik, R. E. and Rodriguez, J. C., Chapter two: Maize. In Crop Post-Harvest: Science and Technology, Volume 2. R. Hodges, and G. Farrell, eds. Ames, Iowa. Blackwell Publishing Ltd. (2004).
 
[5]  Brewbaker, J. L. “Corn production in the tropics: The Hawaii experience”, College of tropical agriculture and human resources University of Hawaii at Manoa. (2003), [http://www.ctahr.hawaii.edu/oc/freepubs/pdf/corn2003.pdf], (Accessed October 2012).
 
Show More References
[6]  Tilahun, S. “Grain based Ethiopian traditional common foods processing science and technology”. In Training module for center of research on grain quality, processing and technology transfer, Haramaya University, Ethiopia. (2007).
 
[7]  Egal, S., Hounsa, A., Gong, Y. Y., Turner, P. C, Wild, C. P., Hall, A. J., Hell, K. & Cardwell, K. F., “Dietary exposure to aflatoxin from maize and groundnut in young children from Benin and Togo, West Africa”, International Journal of Food Microbiology 104(2): 215-224. (2005).
 
[8]  AOAC International, Official Methods of Analysis 17th Ed., Gaithersburg, MD, Method 925.10 (2000).
 
[9]  Hocking, A.D., Pitt, J.I., Samson, R.A. and Thrane, U. (eds). Advances in Food Mycology. Springer Science+Business Media, Inc., 233 Spring Street, New York, NY 10013, USA. 375 pp. 2006a.
 
[10]  Drummond AJ, Ashton B, Buxton S, Cheung M, Cooper A, Heled J, Kearse M, Moir R, Stones-Havas S, Sturrock S, Thierer T and Wilson A (2010) Geneious v5.1, Available from http://www.geneious.com.
 
[11]  Highley E., Wright E.J., Banks H. J. and Champ B.R., ed. (1994). “Stored Product Protection” in Proceedings of the 6th International Working Conference on Stored-product Protection, CAB international, Canberra, volume 2, pages 969-1083.
 
[12]  Walker G. M. and White N. A. Introduction to Fungal Physiology in Fungi Biology and Applications by Kevin Kavanagh (Ed). John Wiley & Sons Ltd, The Atrium, Southern Gate, Chichester, West Sussex PO19 8SQ, England. (2005).
 
[13]  White, T. J., T. Bruns, S. Lee, and J. W. Taylor Amplification and direct sequencing of fungal ribosomal RNA genes for phylogenetics. Pp. 315-322 In: PCR Protocols: A Guide to Methods and Applications, eds. Innis, M. A., D. H. Gelfand, J. J. Sninsky, and T. J. White. Academic Press, Inc., New York. (1990).
 
[14]  Njobeh, P. B., Dutton, M. F., Koch, S. H., Chuturgoon, A., Stoev, S. and Seifert, K., “Contamination with storage fungi of human food from Cameroon”, International Journal of Food Microbiology 135, 193-198. (2009).
 
[15]  Mukvold, G.P. and Desjardins A. E., “Fumonisins in maize: can we reduce their occurrence?” Plant Disease 81: 556-565. (1997).
 
Show Less References