Nucleotide sequence of the gene coding for the 85-B antigen of Mycobacterium leprae

• Published in: Nucleic acids research Vol. 19; no. 20; p. 5789
• Main Authors: DE MENDONCA LIMA, L, CONTENT, J, VAN HEUVERSWYN, H, DEGRAVE, W
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 25.10.1991
• Subjects: 85B antigen; Amino Acid Sequence; Antigens, Bacterial - genetics; Base Sequence; Biological and medical sciences; DNA, Bacterial; Fundamental and applied biological sciences. Psychology; genes; Genes, Bacterial; Genes. Genome; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Mycobacterium leprae; Mycobacterium leprae - genetics; Mycobacterium leprae - immunology; nucleotide sequence; predictions; Sequence Alignment; Antigen; Mycobacterium leprae; Gene; Nucleotide sequence; Mycobacteriales; Mycobacteriaceae; Bacteria; Chromosome DNA; Homology; Actinomycetes; Molecular cloning
• ISSN: 0305-1048; 1362-4962
• DOI: 10.1093/nar/19.20.5789

Antigens of the 85 complex, present in culture supernatants of a variety of mycobacteria, play an important role in humoral and cellular immune responses. As no data on the structure of the corresponding M. leprae proteins were available, we decided to clone the genes coding for the different antigens belonging to this complex. Using a Eag I/BstE II 900 bp DNA fragment coding for part of the M. tuberculosis 32 kDa protein (antigen 85-A; 2) we screened a M. leprae genomic library constructed in the vector lambda-dash. Several clones were isolated and were shown, through hybridization and sequence analysis, to code for antigens 85-A (32 kDa), 85-C (33 kDa) and 85-B (28 kDa, alpha antigen), as judged from sequence homology with the corresponding M. bovis BCG, M. tuberculosis and M. kansasii genes. Here we show that the presumably secreted M. leprae 85-B antigen shares 86.3% and 84.5% homology, respectively, to the M. kansasii and M. bovis BCG corresponding mature antigens. A presumable 38 amino acid signal peptide, as judged by sequence homology and hydrophobicity, precedes the 289 amino acid long mature protein. In the 5' upstream sequence, putative promoter and ribosome binding site sequences could be identified which are homologous to the E. coli consensus.