The Role of The First 14 Amino Acids of Mature M1 Protein of Streptococcus Pyogenes on fibronectin-Binding Activity and Dimer Formation  

Oleh:

Kembaren, Roga Florida ; Ganjara, Adam Reza ; Yurina, Valentina ; Retnoningrum, Debbie Sofie

Jenis: Article from Journal - ilmiah nasional - terakreditasi DIKTI
Dalam koleksi: Microbiology Indonesia vol. 4 no. 1 (Apr. 2010), page 22-26.
Topik: ABS fragment of M 1 protein; dimerization; Fn-binding activity; Non-helical region; Sterptococcus pyogenes
Fulltext: 5.PDF (1.59MB)

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Perpustakaan Pusat (Semanggi) Nomor Panggil: MM78 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada

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Isi artikel

Streptococcus Pyogenesis one of the most important human pathogens which express a multi-facet of virulence factors on its cell surface. One of the virulence factors that has been intensively-studied is the M protein that binds several human proteins. M1 protein, a member of the M protein family, was previously found to bind human fibronectin (Fn), an activity that is responsible for bacterial internalization. A structural study showed that this protein consists of four regions: A.B.S. and C. the study was intended to investigate the role of the first 14 amino acid residues located at the non-helical region of M1 protein in binding Fn, and its ability to form a dimer. The DNA fragment encoding for the ABS protein lacking its first 14 amino acids (ABS?) was cloned into pET-16b, overexpressed Escherichiacoli BL21 (DE30, and protein was purified by affinity chromatography. The purified protein was characterized by sodium dodecyl sulphate polyacrylamide gel electrophoresis and the Fn-binding activtiy was assayed by enzeyme linked immunosorbent assay. The result indicated that the M 1 lacking its first 14 amino acids retains its dimerization and Fn-binding activities.

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