Scanning the Genome of Mycobacterium tuberculosis to Identify Potential Lectins

Singh, DD; Chandran, Divya; Jeyakani, Justin; Chandra, Nagasuma

doi:10.2174/092986607781483813

Cited by 8 publications

(8 citation statements)

References 27 publications

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“…These results are consistent with the varying carbohydrate-binding characteristics observed between different mycobacterial species, as described above [12,74]. While three potential glycan-binding proteins were identified in the Mtb (H37Rv) genome in this study (Table 3) [77], Singh et al, using a different suite of bioinformatic tools, identified eleven, of which nine were annotated as potential lectins [78]. However, most of the proteins encoded by these genes have yet to be biochemically characterized, precluding further functional predictions.…”

Section: Reviewsupporting

confidence: 90%

“…Exceptions are the secreted 13 kDa large lectin from Mtb , sMTL-13 [79–80], and the heparin-binding hemagglutinin (HBHA) [81–85], which have been previously studied in detail (see below). We subsequently discuss the association of the nine putative Mtb lectins identified by Singh et al and Abhinav et al with established lectin families [77–78], such as agglutinin-like sequences (ALS), mannose-sensitive hemagglutinin (MSHA), C-type lectins, and R-type lectins. Furthermore, the filamentous hemagglutinin (FHA) and the heparin-binding hemagglutinin (HBHA) as glycosaminoglycan-binding protein families are also discussed (Table 3, Fig.…”

Section: Reviewmentioning

confidence: 99%

“…Based on bioinformatic analysis, the two Mtb gene products of Rv1753 and Rv2082 were reported to have 27% and 25% amino acid sequence similarity to the ALS1 gene from Candida albicans , which encodes the candida adhesin [78]. This lectin is cell surface-localized and mediates adherence of the fungus to endothelial and epithelial cells [86–87].…”

Section: Reviewmentioning

confidence: 99%

“…Two Mtb gene products, encoded by Rv2813 and Rv3659, were classified as MSHA-like proteins, with the highest amino acid similarity directed to MshM (41%) and MshE (26%), respectively, of the marine bacterium Pseudomonas haloplanktis [78]. These genes encode for proteins involved in assembly of type IV pili (T4P) [91].…”

Section: Reviewmentioning

confidence: 99%

“…The Mtb gene product of Rv2075c shows partial amino acid sequence similarity to mannose-specific C-type lectins from Caenorhabditis elegans , Mus musculus , and Homo sapiens (see Fig. 5 for partial secondary structure prediction and alignment with the human C-type mannose receptor 2) [77–78], and is predicted to be localized to the outer membrane [93]. While Rv2075c orthologues have been identified in all tested Mtb strains ( Mtb H37Ra, Mtb H37Rv, Mtb KZN 1435, Mtb KZN 4207, Mtb CDC1551), no homologous gene was identified in the Mycobacterium africanum strain GM041182 [77].…”

Section: Reviewmentioning

confidence: 99%

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Lectins ofMycobacterium tuberculosis– rarely studied proteins

Kolbe

Veleti

Reiling

2019

Beilstein J. Org. Chem.

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The importance of bacterial lectins for adhesion, pathogenicity, and biofilm formation is well established for many Gram-positive and Gram-negative bacteria. However, there is very little information available about lectins of the tuberculosis-causing bacterium, Mycobacterium tuberculosis (Mtb). In this paper we review previous studies on the carbohydrate-binding characteristics of mycobacteria and related Mtb proteins, discussing their potential relevance to Mtb infection and pathogenesis.

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Section: Reviewsupporting

confidence: 90%

Section: Reviewmentioning

confidence: 99%

Section: Reviewmentioning

confidence: 99%

Section: Reviewmentioning

confidence: 99%

Section: Reviewmentioning

confidence: 99%

See 3 more Smart Citations

Lectins ofMycobacterium tuberculosis– rarely studied proteins

Kolbe

Veleti

Reiling

2019

Beilstein J. Org. Chem.

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Mycobacterium tuberculosis Rv1419 encodes a secreted 13 kDa lectin with immunological reactivity during human tuberculosis

et al. 2010

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In this study, we have identified a secreted 13 kDa lectin from Mtb (Mtb, Mycobacterium tuberculosis; sMTL-13) by homology search of a non-redundant lectin database. Bioinformatic analysis revealed that sMTL-13 belongs to the ricin-type b-trefoil family of proteins containing a Sec-type signal peptide present in Mtb complex species, but not in nontuberculous mycobacteria. Following heterologous expression of sMTL-13 and generation of an mAb (clone 276.B7/IgG1j), we confirmed that this lectin is present in culture filtrate proteins from Mtb H37Rv, but not in non-tuberculous mycobacteria-derived culture filtrate proteins. In addition, sMTL-13 leads to an increased IFN-c production by PBMC from active tuberculosis (ATB) patients. Furthermore, sera from ATB patients displayed high titers of IgG Ab against sMTL-13, a response found to be decreased following successful antituberculosis therapy. Together, our findings reveal a secreted 13 kDa ricin-like lectin from Mtb, which is immunologically recognized during ATB and could serve as a biomarker of disease treatment.

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Identification of mycobacterial lectins from genomic data

2012

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Sixty-four sequences containing lectin domains with homologs of known three-dimensional structure were identified through a search of mycobacterial genomes. They appear to belong to the β-prism II, the C-type, the Microcystis virdis (MV), and the β-trefoil lectin folds. The first three always occur in conjunction with the LysM, the PI-PLC, and the β-grasp domains, respectively while mycobacterial β-trefoil lectins are unaccompanied by any other domain. Thirty heparin binding hemagglutinins (HBHA), already annotated, have also been included in the study although they have no homologs of known three-dimensional structure. The biological role of HBHA has been well characterized. A comparison between the sequences of the lectin from pathogenic and nonpathogenic mycobacteria provides insights into the carbohydrate binding region of the molecule, but the structure of the molecule is yet to be determined. A reasonable picture of the structural features of other mycobacterial proteins containing one or the other of the four lectin domains can be gleaned through the examination of homologs proteins, although the structure of none of them is available. Their biological role is also yet to be elucidated. The work presented here is among the first steps towards exploring the almost unexplored area of the structural biology of mycobacterial lectins.

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Scanning the Genome of Mycobacterium tuberculosis to Identify Potential Lectins

Cited by 8 publications

References 27 publications

Lectins ofMycobacterium tuberculosis– rarely studied proteins

Lectins ofMycobacterium tuberculosis– rarely studied proteins

Mycobacterium tuberculosis Rv1419 encodes a secreted 13 kDa lectin with immunological reactivity during human tuberculosis

Identification of mycobacterial lectins from genomic data

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