ISSN 2736-1756
Perspective
Advanced Journal of Microbiology Research Vol. 2004
Available online at http://internationalscholarsjournals.org/journal/ajmr
© 2004 International Scholars Journals
Perspective
Opportunities in Africa for training in genome science
Daniel K. Masiga1* and Raphael D. Isokpehi2
1International Centre of Insect Physiology and Ecology (ICIPE), P.O. Box 30772, 00100-Nairobi, Kenya.
2South African National Bioinformatics Institute (SANBI), University of the Western Cape, Bellville 7535, South Africa.
Abstract
Genome science is a new type of biology that unites genetics, molecular biology, computational biology and bioinformatics. The availability of the human genome sequence, as well as the genome sequences of several other organisms relevant to health, agriculture and the environment in Africa necessitates the development and delivery of several types and levels of training that will enhance the use of genome data and the associated computational resources. A survey of initiatives that provide opportunities for training in genome science is presented. Current efforts to increase the ability of African scientists to computationally process and analyse genomic and post-genomic data have the potential to produce excellent scientists who perform cutting-edge, hypothesis-based research, and who will accelerate the continent’s scientific and technological development.
Key words: Bioinformatics, computational biology, genome science, networking.
Daniel K. Masiga*, Raphael D. Isokpehi
Page: 1 - 10
Research Article
Advanced Journal of Microbiology Research Vol. 2004
Available online at http://internationalscholarsjournals.org/journal/ajmr
© 2004 International Scholars Journals
Full Length Research Paper
Biolistic transformation of Saccharomyces cerevisiae with β-glucosidase gene from Cellulomonas biazotea
S. Parvez*, Z. Mukhtar, F. Rashid, M.I. Rajoka
National Institute for Biotechnology & Genetic Engineering, P.O. Box 577, Jhang Road, Faisalabad, Pakistan.
Accepted 27 October 2003
Abstract
A β-glucosidase genomic DNA from Cellulomonas biazotea NIAB 442 was isolated and coated onto tungsten microprojectiles for direct transformation of the gene into Saccharomyces cerevisiae. Transformation of β-glucosidase into S. cerevisae conferred the ability to hydrolyse esculin and cellobiose, indicating that the gene is expressed in the bombarded yeast.
Key words: Biolistic transformation, β-glucosidase, Cellulomonas biazotea, Saccharomyces cerevisiae.
F. Rashid, S. Parvez*, M.I. Rajoka, Z. Mukhtar
Page: 1 - 10
Research Article
Advanced Journal of Microbiology Research Vol. 2004
Available online at http://internationalscholarsjournals.org/journal/ajmr
© 2004 International Scholars Journals
Full Length Research Paper
Expression of green fluorescent protein (GFPuv) in Escherichia coli DH5-α, under different growth conditions
Thereza Christina Vessoni Penna*1, Marina Ishii1, Luciana Cambricoli de Souza 1, Olivia Cholewa2
1Department of Biochemical and Pharmaceutical Technology, School of Pharmaceutical Science, University of São Paulo, SP, Brazil.
2Molecular Probes, Inc. Eugene, Or, USA. 97402. Email: [email protected].
Accepted 25 November 2003
Abstract
The recombinant green fluorescent protein (GFPuv) was expressed by transformed cells of Escherichia coli DH5-α grown in LB/amp broth at 37oC, for 8 h and 24 h. To evaluate the effectiveness of different parameters to improve the expression of GFPuv by E. coli, four variable culturing conditions were set up for assays by a fractional factorial (24-1) design at two levels: (i) the effect of storing (24-48 h) the seeded broth at 4oC prior to incubation at 37oC; (ii) the effect of agitation speed (100-200 rpm); (iii) the final concentration (0.05-0.5 mM) of IPTG (isopropyl–β-D-thiogalactopyranoside) and (iv) the addition of IPTG at set cell densities (OD660 0.01-0.8). GFPuv was extracted from cells by the three phase partitioning method (TPP) and further purified with a methyl HIC column. The cultures grown at 37oC/24 h provided the highest yields of GFPuv under the conditions: (i) pre-storage at 4oC/24 h; (ii) agitation speed at 100 rpm; (iii) 0.5 mM IPTG and (iv) IPTG addition at OD660~0.01. On the other hand, at 37oC/ 8 h, GFPuv expression was dependent upon agitation of broth cultures at 200 rpm and the IPTG addition at the beginning of the growth exponential phase.
Key words: Green fluorescent protein (GFPuv), Escherichia coli DH5-α, growth kinetic parameters, expressed GFPuv kinetic parameters, three phase partitioning extraction (TPP).
Luciana Cambricoli de Souza, Olivia Cholewa, Thereza Christina Vessoni Penna*, Marina Ishii
Page: 1 - 10
Research Article
Advanced Journal of Microbiology Research Vol. 2004
Available online at http://internationalscholarsjournals.org/journal/ajmr
© 2004 International Scholars Journals
Full Length Research Paper
Comparative biochemical and molecular evaluation of swarming of Proteus and effects of anti-swarm agents
Iwalokun BA1*, Olukosi YA2, Adejoro A1, Olaye JA1, Fashade O1
1Biochemistry Department, Lagos state University, P.M.B. 1087, Apapa, Lagos, Nigeria.
2Genetics Division, Nigerian Institute of Medical Research (NIMR), 6 Edmond Crescent, Yaba – Lagos, P.M.B. 2013, Lagos, Nigeria.
Accepted 6 December 2003
Abstract
In addition to inadequate understanding of swarming motility and virulence of Proteus, there is paucity of information on the relative effectiveness of the various anti-swarm agents. The anti-swarming effects of urea, sodium dodecylsulphate (SDS) and trihydroxymethylglycine (Tris) on 40 clinical isolates of Proteus Spp. were comparatively investigated and plasmids associated with swarming were characterized. The three substances elicited a comparable concentration-dependent anti-swarming property at 0.25 – 1.25% on nutrient agar. Anti-swarm agents displayed heterogeneity in their ability to cause significant decreases in the expression of virulence factors. Swarm motility was further found to be strongly associated with the expression of virulence factors in these strains. Of the Proteus strains tested, 32 were found to harbour 1 – 4 plasmids of size ranging from 6.0 – 33.5 kb. Plasmid curing resulted in loss of swarming in 65.6% of these strains. In order to reduce the risk of infection with virulent Proteus strains, the laboratory use of urea and SDS is suggested.
Key words: Proteus, swarming, urea, SDS, Tris.
Iwalokun BA*, Olukosi YA, Adejoro A, Fashade O, Olaye JA
Page: 1 - 10
Research Article
Advanced Journal of Microbiology Research Vol. 2004
Available online at http://internationalscholarsjournals.org/journal/ajmr
© 2004 International Scholars Journals
Full Length Research Paper
Characterization of Trypanosoma brucei gambiense stocks isolated from humans by RAPD fingerprinting in Côte d’Ivoire: Another evidence for multiple infections
Bruno Oury1, Vincent Jamonneau2, Michel Tibayrenc1, Philippe Truc3*
1Institut de Recherche pour le Développement (IRD), Research Unit 165 "Génétique et Evolution des Maladies
Infectieuses" UMR CNRS/IRD 2724, BP 64501 34394 Montpellier cedex 5, France.
2Institut de Recherche pour le Développement (IRD), Research Unit 35 Trypanosomoses Africaines, Institut Pierre Richet, BP 1500, Bouaké, Côte d’Ivoire.
3Institut de Recherche pour le Développement, IRD, Research Unit 35 BP 1857, Organisation de Coordination pour la lutte contre les Endémies en Afrique Centrale (OCEAC), Department of Research and Control of Human African Trypanosomiasis, BP 288, Yaounde, Cameroon.
Accepted 3 December 2003
Abstract
Trypanosoma brucei gambiense was isolated twice from each of 23 patients in Côte d’Ivoire. Genetic characterization using RAPD (Random Primed Amplified Polymorphic DNA) showed additional variability within a given isoenzyme profile (zymodeme), confirming that this fingerprinting method has a higher discriminative power (faster molecular clock) than isoenzymes. RAPD confirmed also the evidence of multiple infections by different genotypes in the same patient despite a low genetic variability among Trypanosoma brucei gambiense stocks. The involvement of this phenomenon in treatment failure is discussed.
Key words: Human African Trypanosomiasis, Trypanosoma brucei gambiense, RAPD, multiple infections.
Michel Tibayrenc, Vincent Jamonneau, Philippe Truc*, Bruno Oury
Page: 1 - 10
Research Article
Advanced Journal of Microbiology Research Vol. 2004
Available online at http://internationalscholarsjournals.org/journal/ajmr
© 2004 International Scholars Journals
Full Length Research Paper
The effects of aluminium and selenium supplementation on brain and liver antioxidant status in the rat
M. G. Abubakar1*, A. Taylor2 and G. A. Ferns2
1Department of Biochemistry Usmanu Danfodiyo University P.M.B. 2346 Sokoto, Nigeria.
2School of Biomedical & Life Sciences, University of Surrey, Guildford Surrey GU2 7XH UK.
Accepted 28 October 2003
Abstract
This in vivo study was designed to investigate the potential of aluminium (Al), in the absence of added iron, to participate in either antioxidant or pro-oxidant events. Some markers of oxidative stress were determined in liver and brain of rats exposed to aluminium lactate, either alone or in the presence of dietary supplements of selenium (se) as selenite. Exposure to aluminium for 21 days resulted in a statistically significant (P<0.05) decrease in brain glutathione. However, a non-significant increase in hepatic glutathione was observed in animals supplemented with either Se or Al, but Al in combination with Se prevented this elevation. In the brain a statistically non-significant increase (P>0.05) was observed in the GSH content. Contrary to what is known, Al exposure resulted in statistically significant decrease (P<0.001) in lipid peroxidation as measured by production of malondialdehyde in both liver and brain. Aluminium exposure had no significant effect on the liver and brain superoxide dismutase activity. Results of the present study suggest that in rat aluminium exposure may have both pro-oxidant and antioxidant effect. Furthermore, Se supplementation may offer some protection against aluminium toxicity but this needs to be further elucidated.
Key words: Aluminium, selenium, rat, brain, liver, antioxidant enzymes.
M. G. Abubakar*, A. Taylor and G. A. Ferns
Page: 1 - 10