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Annales Bogorienses
Published by Badan Riset dan Inovasi Nasional
ISSN : 05178452     EISSN : 24077518     DOI : https://doi.org/10.55981/ann.bogor
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Annales Bogorienses aims to disseminate high-quality scientific research in the field of life sciences, with a strong emphasis on advancing knowledge and applications in biotechnology, molecular biology, biochemistry, bioinformatics, and bioengineering. The journal serves as a platform for researchers, academicians, and practitioners to share original findings, innovative methodologies, and critical reviews that contribute to scientific progress and sustainable development. The journal covers research in biotechnology, molecular biology, biochemistry, bioinformatics, and bioengineering. It publishes original research articles, reviews, and short communications, and is committed to rigorous peer review and open access for the widest possible dissemination of scientific knowledge.
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Articles 6 Documents
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Search results for , issue "Vol. 14 No. 2 (2010): Annales Bogorienses" : 6 Documents clear
EDITOR'S PREFACE Lisdiyanti, Puspita
Annales Bogorienses Vol. 14 No. 2 (2010): Annales Bogorienses
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Conservation of Major L1 and Variability of Minor L2 Capsid Late Protein Genes in Human Papillomavirus of Indonesia Variants Nuswantara, Sukma; Prana, Titik K.; Wulandari, Dwi; Widyowati, Henni; Anzela, Vera; Levy, Dea; Cahyadi, Petrus; Tjandra, Lukas D
Annales Bogorienses Vol. 14 No. 2 (2010): Annales Bogorienses
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Human Papilloma Virus (HPV) has an outstanding feature for its vast intraspecies variability. Of all known 100 types or more, 15 types of them are classified as high risk because of their occurrence in more than 95% of cervical cancer cases. Among all genes in their genome, E6 and E7 genes are considered oncogenes and have close relevance with their pathogenicity, whilst L1 and L2 genes produce capsid proteins that directly interact with their host receptors. Considering the importance of L1 and L2 in host-receptor relationship, we tried to investigate their molecular variability thereby uncover their specificity as Indonesian variants. Here we reported about the conservation of L1 minor capsid protein and variability of L2 capsid protein among high-risk types Human Papilloma Virus (HPV). The results indicated that L1 DNA was relatively more conserved than its L2 counterpart. Also it was indicated that the middle part of either L1 or L2 CDS‟ showed more DNA variability than those at their upstream sequences. It is concluded that L2 middle sequences are important factors for intraspecific variations found in HPV of Indonesian variants.
The Development of A Bioassay Based on Heterologous Expression of M2 Ion-Channel Protein Prasetyoputri, Anggia; Yuliaty, Neti; Tuharea, Warda; Febyanti, Alisin; Sunarko, Bambang; Atmosukarto, Ines I. C.
Annales Bogorienses Vol. 14 No. 2 (2010): Annales Bogorienses
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Emerging resistant viral strains combined with the limited availability of antivirals in a pandemic scenario highlight the need for the development of novel influenza antivirals. A bioassay based on the M2 protein of influenza virus - a potential target for antivirals - was developed to screen endophytic microbial extracts. M2 can be synthesized using PCR, thus eliminating the need for the handling of infectious specimen. Following cloning of the M2 gene into a pET backbone, the resultant plasmid was transformed into BL21 (DE3) pLyss E. coli cells. Cultures of these cells were set up at 37C following inoculation with a starter culture, to reach an OD at 600nm (OD600) of 0.4-0.6. Once at the required OD, the culture was split in two aliquots and expression of the M2 protein was induced in one of the duplicates with the addition of isopropyl β-D-thiogalactopyranoside (IPTG). Bacterial growth was monitored at 60-minute intervals. Exogenous expression of the M2 protein has been reported to decrease host cells viability, resulting in lower OD600 values. Our results suggest that the M2 protein was expressed and that overexpression of this protein resulted in consistently lower OD600 values of induced cultures compared with that of uninduced cultures. Based on this principle, extracts can be screened for their ability to block M2 function as identified by increased OD600 values.
Construction of pY-Af Vector for Expression of Thermostable α-L-Arabinofuranosidase in Saccharomyces cerevisiae Wirajana, I Nengah; Puspaningsih, Ni Nyoman Tri; Wasito, Eddy Bagus; Kusuma, Soekry Erfan; Kimura, Tetsuya; Sakka, Kazuo
Annales Bogorienses Vol. 14 No. 2 (2010): Annales Bogorienses
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In this research, construction of expression vector for thermostable α-L-arabinofuranosidase in Saccharomyces cerevisiae BJ1824 was conducted. The Escherichia coli/S. cerevisiae shuttle vector, pYES2 was used as parental vector in construction. The abfA gene encoding α-L-arabinofuranosidase from Geobacillus thermoleovorans IT-08 was amplified by PCR, in which the plasmid pTP510 was used as a template. The amplification product was treated with SacI and XhoI and then subcloned to the pYES2 vector, which was previously digested with SacI and XhoI. The recombinant plasmid was designated as pY-Af and propagated first in E. coli Top10, and then transformed into S. cerevisiae BJ1824. For α-Larabinofuranosidase (AbfA) production, the yeast transformants were grown in YNBG selective medium and YPG rich medium, using galactose as an inducer. The AbfA activity was assayed by measuring the amount of p-nitrophenol (pNP) released from p-nitrophenyl-α-L-arabinofuranoside (pNPA) substrate at pH 6.0 and 70oC for 30 min. The recombinant AbfA activity was detected in either of culture medium (0.98%), cellassociated (14.17%) and intracellular (84.85%) when recombinant yeast was grown in YPG rich medium.
Improvement of Genetic Transformation Efficiency in Vanda tricolor Orchid Using Acetosyringone Dwiyani, Rindang; Purwantoro, Azis; Indrianto, Ari; Semiarti, Endang
Annales Bogorienses Vol. 14 No. 2 (2010): Annales Bogorienses
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Vanda tricolor Lindl. var. suavis is an Indonesian wild orchid which is now extremely rare in nature due to its habitat destruction. Development of an appropriate method for improving Vanda orchid through genetic modification could be valuable for horticulture and, indirectly, also for conservation. In this research, a method of Agrobacterium-mediated transformation of two V. tricolor obtained from Salak Mount, West Java and Merapi Mount, Yogyakarta in Indonesia protocorms was improved using acetosyringone (AS). Concentrations of 0 and 25 ppm AS were used in transformation of pG35S binary vector containing kanamycin resistance geneinto V. tricolor protocorms. The result showed that 25 ppm AS was required on inoculation with Agrobacterium solution, without AS on cocultivation. Five weeks after treatment on the 300 ppm kanamicyn containing medium, green protocorms were obtained, that was 11.01% for V. tricolor from Salak Mount with pre-culture treatment prior to inoculation, 9.39% for V. tricolor from Merapi Mount with pre-culture treatment prior to inoculation, and 1.37% for V. tricolor from Merapi Mount without pre-culture treatment prior to inoculation. The best condition to set high efficiency of transformation is pre-culture protocorms prior inoculation, soaking protocorm on 25 ppm AS for 30 minutes, then co-cultivate its on AS-free callus induction medium.
Site-Directed Mutagenesis of Glu-269 L-Arabinose Isomerase from Geobacillus stearothermophilus Isolated from Tanjung Api Poso, Indonesia Fitriani, Dewi; Wulandari, Puspita Suci; Saksono, Budi
Annales Bogorienses Vol. 14 No. 2 (2010): Annales Bogorienses
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Abstract

Industrializing of tagatose requires enzymes that meet to industrial need such as thermophile, slightly acidic and metal independent. Previously, we cloned, sequenced and expressed L-arabinose isomerase from Geobacillus stearothermophilus isolated from Tanjung Api, Poso, Indonesia. Based on DNA alignment analysis, the gene had high homology with those of G. stearothermophilus T6 (Gene Bank Acc No: AAD45718) which has optimum activity at high temperature and alkaline condition. In this paper, we described site-directedmutagenesis approach to mutate Glu-269 (Q269) to Lys-269 (K269) to decrease the optimum pH of the strain. Sequencing result showed that mutagenesis had been successful to mutate amino acid at position 269 from glutamine (Q) into lysine (K). Expression of mutant Q269 showed protein with molecular mass ~56 kDa.

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