Lpp34, a Novel Putative Lipoprotein from Mycobacterium avium subsp.

GIOFFRÉ, ANDREA; ZUMÁRRAGA, MARTÍN; MEIKLE, VIRGINIA; MORCELLA, CLAUDIA; BIGI, FABIANA; ALITO, ALICIA; CAIMI, KARINA; SANTANGELO, MARÍA DE LA PAZ; PAOLICCHI, FERNANDO; ROMANO, MARÍA ISABEL; CATALDI, ANGEL

J Vet Med B Infect Dis Vet Public Health.

Blackwell Verlag

Lugar: Berlin; Año: 2006 vol. 53 p. 34 - 41

0931�1793

A Mycobacterium avium subsp. paratuberculosis expression library in lambda ZAP was screened with immunized mice sera. One clone was selected, sequenced and further characterized. The sequence analysis of the hypothetical open-reading frame (ORF) predicts a protein of 20.8 kDa with a probable signal sequence compatible with Cys-acylation at Cys24, characteristic of lipoproteins. In consequence, the protein was termed Lpp34. Recombinant expression of Lpp34 was achieved by cloning the lpp34 gene into the histidine-tag expression vector pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis library in lambda ZAP was screened with immunized mice sera. One clone was selected, sequenced and further characterized. The sequence analysis of the hypothetical open-reading frame (ORF) predicts a protein of 20.8 kDa with a probable signal sequence compatible with Cys-acylation at Cys24, characteristic of lipoproteins. In consequence, the protein was termed Lpp34. Recombinant expression of Lpp34 was achieved by cloning the lpp34 gene into the histidine-tag expression vector pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis library in lambda ZAP was screened with immunized mice sera. One clone was selected, sequenced and further characterized. The sequence analysis of the hypothetical open-reading frame (ORF) predicts a protein of 20.8 kDa with a probable signal sequence compatible with Cys-acylation at Cys24, characteristic of lipoproteins. In consequence, the protein was termed Lpp34. Recombinant expression of Lpp34 was achieved by cloning the lpp34 gene into the histidine-tag expression vector pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis library in lambda ZAP was screened with immunized mice sera. One clone was selected, sequenced and further characterized. The sequence analysis of the hypothetical open-reading frame (ORF) predicts a protein of 20.8 kDa with a probable signal sequence compatible with Cys-acylation at Cys24, characteristic of lipoproteins. In consequence, the protein was termed Lpp34. Recombinant expression of Lpp34 was achieved by cloning the lpp34 gene into the histidine-tag expression vector pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis library in lambda ZAP was screened with immunized mice sera. One clone was selected, sequenced and further characterized. The sequence analysis of the hypothetical open-reading frame (ORF) predicts a protein of 20.8 kDa with a probable signal sequence compatible with Cys-acylation at Cys24, characteristic of lipoproteins. In consequence, the protein was termed Lpp34. Recombinant expression of Lpp34 was achieved by cloning the lpp34 gene into the histidine-tag expression vector pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis Mycobacterium avium subsp. paratuberculosis expression library in lambda ZAP was screened with immunized mice sera. One clone was selected, sequenced and further characterized. The sequence analysis of the hypothetical open-reading frame (ORF) predicts a protein of 20.8 kDa with a probable signal sequence compatible with Cys-acylation at Cys24, characteristic of lipoproteins. In consequence, the protein was termed Lpp34. Recombinant expression of Lpp34 was achieved by cloning the lpp34 gene into the histidine-tag expression vector pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosis lpp34 gene into the histidine-tag expression vector pRSET-A. Western blot analysis showed a protein band with a molecular weight of 34 kDa. The native protein was localized in the membrane fraction of M. avium subsp. paratuberculosisM. avium subsp. paratuberculosis and extracted in the detergent phase of Triton X-114. Southern blot and polymerase chain reaction showed that the gene is absent from all the non-M. avium complex mycobacterial genomes tested. Humoral reactivity using bovine sera demonstrated that this protein is widely recognized by both the infected and non-infected animals. This could partly be due to the conserved sequence in close-related environmental bacteria such as M. avium subsp. avium and to the presence of a conserved epitope in other bacteria such as Escherichia coli. In conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. epitope in other bacteria such as Escherichia coli. In conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. epitope in other bacteria such as Escherichia coli. In conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. epitope in other bacteria such as Escherichia coli. In conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. epitope in other bacteria such as Escherichia coli. In conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. tested. Humoral reactivity using bovine sera demonstrated that this protein is widely recognized by both the infected and non-infected animals. This could partly be due to the conserved sequence in close-related environmental bacteria such as M. avium subsp. avium and to the presence of a conserved epitope in other bacteria such as Escherichia coli. In conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. epitope in other bacteria such as Escherichia coli. In conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. epitope in other bacteria such as Escherichia coli. In conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. epitope in other bacteria such as Escherichia coli. In conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. mycobacteria and absent in the M. tuberculosis complex. conclusion, these findings show that Lpp34 is a membrane protein and a putative lipoprotein present in M. avium complex mycobacteria and absent in the M. tuberculosis complex. myco