AbstrakKanker serviks disebabkan oleh infeksi kronik human papillomavirus (HPV) dengan genotipe HPV-16 sebagai HPV tersering yang menginfeksi epitel serviks. Protein penyelubung virus yang disebut kapsid mayor (L1) mempunyai peranan penting dalam menginfeksi epitel serviks. Tujuan penelitian untuk mengisolasi dan menganalisis sekuens gen L1 Sequence of Human Papilomavirus 16 Major Capsid L1 Gene from Clinical Isolates in Bandung AbstractCervical cancer is strongly associated with chronic human papillomavirus (HPV) infection. HPV-16 is the most prevalent genotype infecting cervical epithelium. The major coat protein of viral particle (L1) plays a key role in the infection process. Our study aimed to isolate the HPV-16 L1 gene and analyze its sequence. Samples used were samples collected from the Department of Obstetrics and Gynaecology, Dr. Hasan Sadikin General Hospital, Bandung during the period of June to October 2010. In this study, the HPV-16 L1 sequence was analyzed from the viral deoxyribonucleic acid (DNA) extracted from biopsy sample of cervical cancer patient biopsy samples. The HPV-16 L1 amplification was performed using the polymerase chain reaction with specific primer. The HPV infection in the cervical tissue was confirmed by commercial HPV genotyping test. The L1 fragment was cloned into plasmid and the insert of the recombinant clone pJET1.2/L1-16 was digested using BamHI and BgIII. The amplicon result showed HPV-16 L1 gene with a length of 1.595 base pairs. The sequence analysis of two samples using software BIOEDIT dan Basic Local Alignment Search Tool revealed a high level of sequence similarity to L1 HPV-16 from Thailand (99% and 97%) as registered in GenBank. In conclusion, the L1 HPV-16 gene from Bandung isolates revealed variations from published sequence. Knowledge on L1 gene sequence may give additional information to the development of vaccine. Further study on vaccine development is currently ongoing using this HPV-16 clone that may be specific to Indonesian population. [MKB. 2014;46(3):143-49]

Post-translational protein import into organelles is an important process to maintain cellular functions. During preprotein transport in the cytosol, chaperones, such as heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90), are functioning to prevent aggregation and to maintain the correct protein folding of preproteins. This research was conducted in order to understand the chaperone-mediated, post-translational import of preproteins into the endoplasmic reticulum of Arabidopsis thaliana. AtTPR7 (Arabidopsis thaliana Tetratrico Peptide Repeat 7) is found in the endoplasmic reticulum and contains TPR domain, which mediates protein interaction with cytosolic Hsp70 and Hsp90. In this study, recombinant AtTPR7 was expressed in E. coli BL21 (DE3)-RIPL cells and purified using an N-terminal His-tag. In order to study the interactions of the protein with the chaperones, we used pulldown and Western blot assays. We could thereby show that the N-terminally His-tagged AtTPR7 protein interacted with Hsp70 and Hsp90.