It gives me great pleasure to wish all our readers a very happy new year. I’m very happy to inform you that this year will also see a lot of positive changes to the journal and its services.

This year sees the APJMBB returning to its quarterly format to enable more high quality papers to be published. We also seek to offer improved services to our authors in the form of a streamlined review process and rapid time to publication with the four issue format. By the year end we will be instituting an online review process which will further enhance the efficiency of our services. While we will maintain our open access online format, from this year a limited print subscription will also be available for libraries and individuals.

A highlight for this year will be our Focus issue in July on Transgenic Insects with guest editor Dr Seshadri Vassan from the U.K. The issue will highlight advances by international experts in the form of reviews, commentaries and research papers on multidisciplinary aspects of the topic. The special issue is yet another change to the journal which will allow us to focus on high impact areas in the field of molecular biology and biotechnology.

To celebrate the many changes of the APJMBB and as part of the anniversary celebrations of the MSMBB (this year the parent society of the journal, the Malaysian Society for Molecular Biology and Biotechnology will also launch its 20th Anniversary Celebrations) page charges will be waived and authors will receive one complimentary print copy of the journal. This has been made possible by support from many quarters.

Last year saw both exciting and distressing developments in the world not only in science but in many events which have affected the daily lives of many of us. Scientific advancement has an important role to play in the future direction of many communities and economies and timely and accurate dissemination and communication of knowledge remains at the fore­front of these endeavors. It too remains the philosophy of the APJMBB as we approach the end of the 10th year of the new millennium and for this we look forward to your continued support and readership.

Rofina Yasmin Othman PhD
Chief Editor
Asia Pacific Journal for Molecular Biology and Biotechnology

Email: This email address is being protected from spambots. You need JavaScript enabled to view it.

*Author for Correspondence.
Department of Immunology,
School of Medical Sciences,
University Science Malaysia,
16150 Kubang Kerian, Kelantan,
Malaysia.
Tel: 609 766 4220; Fax: 609 765 3370;
Email: This email address is being protected from spambots. You need JavaScript enabled to view it.

Abstract.
In this study, a plasmid DNA encoding Mtb8.4, 30kDa (Ag85B) and 32kDa (Ag85A) genes of M. tuberculosis was constructed as an alternative vaccine candidate against TB. Using assembly polymerase chain reaction (PCR) method, the syn­thetic gene, designated as VacIV, was constructed from overlapping oligonucleotides of the desired genes. The VacIV gene was cloned into an expression vector, pVAX1© to produce a DNA vaccine candidate namely pVaxVacIV. The immunogenicity of pVaxVacIV was then tested in mice. Mice were immunized intramuscularly with pVaxVacIV. Control mice were immunized with the blank vector (pVAX1©). The splenocytes were cultured with purified protein derivatives (PPD), rVacIV protein or Mtb8.4 synthetic peptide for lymphocytes transformation test (LTT) and cytokines assay. Sera were also collected to determine the level of serum IgG subclasses. Our results showed that lymphocytes from mice immunized with the pVaxVacIV secreted significantly higher level of interferon gamma (IFN-γ) but not Interleukin-4 (IL-4) compared to the control mice. Mice immunized with pVaxVacIV also showed high stimulation index and high ratio of IgG2a:IgG1 as compared to control group. These results sug­gested that pVaxVacIV immunogenic in mice and can be further developed as a potential vaccine candidate for TB.

*Author for Correspondence.
Chemistry Department,
Faculty of Science,
Univer­sity of Malaya, 50603
Kuala Lumpur, Malaysia.
Tel: (603)79674254; Fax: (603)79674193;
Email: This email address is being protected from spambots. You need JavaScript enabled to view it.

Abstract.
Electrostatic potential calculations were performed in order to understand the effect of long-range electrostatic interac­tions of L-arginine, L-canavanine and L-citrulline in binding to the Escherichia coli arginine repressor C-terminal domain (ArgRc. The three ligands were also subjected to the same studies while bound to a mutant protein, ArgRc(D128N). The results showed significant changes in the electrostatic potential of ArgRc and ArgRc(D128N) due to L-arginine binding while no significant changes were observed for ArgRc and ArgRc(D128N) bound to either L-canavanine or L-citrulline. The study also revealed changes in the electrostatic potential of ArgRc(D128N) that may explain the ability of ArgRc(D128N) to act as a superrepres­sor.

*Author for Correspondence.
Department of Biochemistry,
Faculty of Science,
Mahidol University,
Bangkok 10400, Thailand.
Tel: +66-2-2015600 ; Fax: +66-2-3547174;
Email: This email address is being protected from spambots. You need JavaScript enabled to view it.

Abstract.
A total of 12,520 lactic acid bacteria (LAB) isolated from fermented fish products “som-fak” were screened for bac­teriocin. One Lactobacillus plantarum PMU33 strain produced bacteriocin that inhibited a large number of Gram-positive bacteria including food borne pathogens, Listeria monocytogenes, Bacillus cereus and Staphylococcus aureus. Biochemical studies revealed that the bacteriocin was heat stable even at autoclaving temperature (121°C for 15 min) and was active over a wide pH range (2-10). The bacteriocin purified and characterized from the culture supernatant consists of two peptides with the molecular masses of 3222 and 3099 by mass spectrometry analysis. The molecular mass of this two-peptide bacteriocin were nearly identical to that of two-peptide plantaricin W (Plw) which consists of two peptides Plwα and Plwβ. The genes encoding these two peptides ampli­fied by PCR with Plw gene specific primer showed identical sequences to Plwα and Plwβ. The bacteriocins and their producing strains isolated from som-fak may find application as bio-preservatives in fermented food products.