Characterization of the Gene Encoding the MPB51, One of the Major Secreted Protein Antigens of Mycobacterium bovis BCG, and Identification of the Secreted Protein Closely Related to the Fibronectin Binding 85 Complex

Ohara, Naoya; Kitaura, Hideki; Hotokezaka, Hitoshi; Nishiyama, Takeshi; Wada, Naoko; Matsumoto, Sohkichi; Matsuo, Takemitsu; Naito, Mariko; Yamada, Takeshi

doi:10.1111/j.1365-3083.1995.tb03589.x

Cited by 47 publications

(44 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The primary structure is highly conserved at this region. For example, M. kansasii and M. tuberculosis sequences varied in only three out of 30 amino acids in this region [31]. However the second and tertiary structures may not always be conserved completely.…”

Section: B-cell Epitope Of Amentioning

confidence: 99%

Immunological Characterization of α Antigen of Mycobacterium kansasii: B‐Cell Epitope Mapping

et al. 1998

View full text Add to dashboard Cite

Naito M, Ohara N, Matsumoto S, Yamada T. Immunological Characterization of a Antigen of Mycobacterium kansasii: B-Cell Epitope Mapping. Scand J Immunol 1998;48:73-78 Mapping of B-cell epitopes on a antigen of Mycobacterium kansasii (K-a) was carried out by using recombinant truncated K-a fusion peptides. We observed that two immunodominant B-cell epitopes (amino acids 222-268 and 267-306) and one minor epitope (amino acid 249-286) were located in the C-terminal region of K-a. The other three minor B-cell epitopes were mapped in N-terminal (amino acids 80-98 and 99-166) and central (amino acid 174-204) regions of K-a. All defined epitopes were common to Mycobacterium tuberculosis and M. kansasii. Besides these common epitopes, a region in K-a (amino acid 290-319) revealed different reactivities between antibodies against K-a and a antigen of M. tuberculosis. These findings may provide a basis for development of serodiagnosis that can distinguish between M. kansasii and M. tuberculosis infections.

show abstract

Section: B-cell Epitope Of Amentioning

confidence: 99%

Immunological Characterization of α Antigen of Mycobacterium kansasii: B‐Cell Epitope Mapping

et al. 1998

View full text Add to dashboard Cite

show abstract

“…FbpD) (43) and ModD (44,45). Binding to Fn, likely a significant factor in the virulence of mycobacteria, represents a potential first step in the attachment and entry of mycobacteria into host cells.…”

Section: Volume 287 • Number 3 • January 13 2012mentioning

confidence: 99%

Novel Mycobacteria Antigen 85 Complex Binding Motif on Fibronectin

Kuo

Bell

Hsieh

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

“…The antigen 85A (Ag85A), a member of the Ag85 protein complex (Ag85A,-B and-C) with mycolyltransferase activity, represents one of the most potent antigens and a lead vaccine candidate (Huygen et al, 1996). The antigen MPT51/MPB51 (mycobacterial protein secreted by M. bovis, BCG/mycobacterial protein secreted by M. tuberculosis) binds fibronectin and elicits strong immune responses (Ohara et al, 1995). For the work presented here, we used "firstgeneration" peptide microarray slides containing 15 mer peptides, with 5 aa overlaps, which cover the entire proteins listed in Table 2.…”

Section: Peptidesmentioning

confidence: 99%

Validation of peptide epitope microarray experiments and extraction of quality data

Nahtman

Jernberg

Mahdavifar

et al. 2007

Journal of Immunological Methods

View full text Add to dashboard Cite

Introduction: Within the last decade, the development of antigen microarray slides has enabled the simultaneous measurement of serum reactivity to hundreds of peptides in a single biological sample. Despite this considerable scientific progress, many issues remain regarding the quality, analysis and interpretation of the data these slides produce. There is currently no accepted approach to guide data analysis, and researchers use a wide variety of statistical methods and software tools. We designed and implemented a laboratory experiment to assess the reliability and range of measurement of peptide microarray data, and present graphical and statistical procedures for pre-processing so that quality data can be extracted for addressing biological hypotheses. Methods: Synthetic peptides spanning the proteins Ag85A, Ag85B, CFP10, MPT51/MPB51, TB10.4 and ESAT-6 were chosen as a paradigm to screen for serum reactivity to Mycobacteria tuberculosis (MTB). We explored various quantitative and graphical methods for presenting the responses from a slide. We replicated assays of samples from five TB-positive individuals to examine reproducibility, and used linear mixed models to investigate the various sources of variability, and to assess the range of measurement. We use our methods to extract data from the five TB-positive individuals and five healthy controls, and analyse the "normalized" responses using the freely available SAM package. Results: The ratio of foreground to background signal (on a log scale) provides an appropriate response index. A two-dimensional graphical display clearly illustrates the responses from the control and peptide features on a slide. Mixed model analysis of the replicated slides found a high reproducibility of the assay between operators, days and experiments. The range of measurement was also satisfactory. Our analysis of the normalized responses from the five TB-positive patients and five healthy controls suggested that 10 of the 363 peptides assessed had significantly higher responses in the TB-positive group. Conclusions: Carefully designed laboratory experiments and rigorous statistical analysis can enable the removal of technical artefacts to produce quality peptide array data for addressing biological hypotheses. These instruments, which enable valid Journal of Immunological Methods 328 (2007) 1 -13 www.elsevier.com/locate/jim Abbreviations: TB, tuberculosis; MTB, mycobacteria tuberculosis, M.tuberculosis (M.tub); MOTT, mycobacteria other than tuberculosis (MOTT); ESAT-6, early secreted antigenic target 6-kDa protein; FCS, fetal calf serum; FDR, false discovery rate; CFP10, culture filtrate protein 10; Ag85A, antigen 85A, a member of the Ag85 protein complex (Ag85A,-B, -C) comparisons across slides and/or batches of slides, will escort future comparative analyses targeting high content serum reactivity profiling against a broad array of B-cell epitopes.

show abstract

Characterization of the Gene Encoding the MPB51, One of the Major Secreted Protein Antigens of Mycobacterium bovis BCG, and Identification of the Secreted Protein Closely Related to the Fibronectin Binding 85 Complex

Cited by 47 publications

References 42 publications

Immunological Characterization of α Antigen of Mycobacterium kansasii: B‐Cell Epitope Mapping

Immunological Characterization of α Antigen of Mycobacterium kansasii: B‐Cell Epitope Mapping

Novel Mycobacteria Antigen 85 Complex Binding Motif on Fibronectin

Validation of peptide epitope microarray experiments and extraction of quality data

Contact Info

Product

Resources

About