Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl

PL EN


Preferences help
enabled [disable] Abstract
Number of results
2015 | 62 | 2 | 191-196

Article title

Identification of proteins associated with Mycobacterium tuberculosis virulence pathway by their polar profile

Content

Title variants

Languages of publication

EN

Abstracts

EN
With almost one third of the world population infected, tuberculosis is one of the most devastating diseases worldwide and it is a major threat to any healthcare system. With the mathematical-computational method named "Polarity Index Method", already published by this group, we identified, with high accuracy (70%), proteins related to Mycobacterium tuberculosis bacteria virulence pathway from the Tuberculist Database. The test considered the totality of proteins cataloged in the main domains: fungi, bacteria, and viruses from three databases: Antimicrobial Peptide Database (APD2), Tuberculist Database, Uniprot Database, and four antigens of Mycobacterium tuberculosis: PstS-1, 38-kDa, 19-kDa, and H37Rv ORF. The method described was calibrated with each database to achieve the same performance, showing a high percentage of coincidence in the identification of proteins associated with Mycobacterium tuberculosis bacteria virulence pathway located in the Tuberculist Database, and identifying a polar pattern regardless of the group studied. This method has already been used in the identification of diverse groups of proteins and peptides, showing that it is an effective discriminant. Its metric considers only one physico-chemical property, i.e. polarity.

Year

Volume

62

Issue

2

Pages

191-196

Physical description

Dates

published
2015
received
2014-08-21
revised
2015-02-01
accepted
2015-04-19
(unknown)
2015-05-28

Contributors

  • Departamento de Matemáticas, Facultad de Ciencias, Universidad Nacional Autónoma de México, C.P. 04510 D.F., México
  • Unidad de Cuidados intensivos y Unidad de Investigación Biomédica. Hospital Juárez de México, C.P. 07760 D.F., México
author
  • Departamento de Inmunologia, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, C.P. 04510 D.F., México
author
  • Centro de Investigaciones Químicas, Universidad Autónoma del Estado de Morelos, C.P. 62209 Chamilpa, Cuernavaca, Morelos, México
  • Departamento de Matemáticas, Facultad de Ciencias, Universidad Nacional Autónoma de México, C.P. 04510 D.F., México
  • Facultad de Ciencias de la Salud, Universidad Anahuac. C.P. 52786 Huixquilucan Estado de Mexico, México
author
  • Facultad de Ciencias de la Salud, Universidad Anahuac. C.P. 52786 Huixquilucan Estado de Mexico, México

References

  • Alteri CJ, Xicohténcatl-Cortes J, Hess S, Caballero-Olín G, Girón JA, Friedman RL (2006) Mycobacterium tuberculosis produces pili during human infection. Proc Natl Acad Sci USA 104: 5145-5150.
  • BIW (2010) Broad Institute website
  • Diaz-Silvestre H, Espinosa-Cueto P, Sanchez-Gonzalez A, Esparza-Ceron MA, Pereira-Suarez AL, Bernal-Fernandez G, Espitia C, Mancilla R (2005) The 19-kDa antigen of Mycobacterium tuberculosis is a major adhesin that binds the mannose receptor of THP-1 monocytic cells and promotes phagocytosis of mycobacteria. Microb Pathog 39: 97-107.
  • Dye C, Scheele S, Dolin P, Pathania V, Raviglione MC (1999) Consensus statement. Global burden of tuberculosis: estimated incidence, prevalence, andmortality by country. WHO Global Surveillance and Monitoring Project. JAMA 282: 677-686.
  • Esparza M, Palomares B, García T, Espinosa P, Zenteno E, Mancilla R (2015) PstS-1, the 38-kDa mycobacterium tuberculosis glycoprotein, is an adhesin, which binds the macrophage mannose receptor and promotes phagocytosis. Scand J Immunol 81: 46-55.
  • Klemm P, Schembri MA (2000) Bacterial adhesins: function and structure. Int J Med Microbiol 290: 27-35.
  • Lew JM, Kapopoulou A, Jones LM, Cole ST (2011) TubercuList-10 years after. Tuberculosis (Edinb) 91: 1-7.
  • Magrane M, The UniProt consortium (2011) UniProt Knowledgebase: a hub of integrated protein data Database bar009 accessed Oct 21, 2013.
  • Pauling L (1955) General Chemistry, 3rd edn, W. H. Freeman and Company Publishers, San Francisco, USA.
  • Polanco C, Buhse T, Samaniego JL, Castañón-González JA (2013) Detection of selective antibacterial peptides by the Polarity Profile method. Acta Biochim Pol 60: 183-189.
  • Polanco C, Castañón-González JA, Samaniego JL (2014c) Comment to: Arabi YM, Arifi AA, Balkhy HH, Najm H, Aldawood AS, Ghabashi A, Hawa H, Alothman A, Khaldi A, Raiy B (2014c) Clinical Course and outcomes of critically ill patients with middle east respiratory syndrome coronavirus infection. Ann Intern Med
  • Polanco C, Samaniego JL (2009) Detection of selective cationic amphipatic antibacterial peptides by Hidden Markov models. Acta Biochim Pol 56: 167-176.
  • Polanco C, Samaniego JL, Buhse T, Mosqueira FG, Negron-Mendoza A, Ramos-Bernal S, Castañón-González JA (2012) Characterization of selective antibacterial peptides by polarity Index. Int J Peptides 58502
  • Polanco C, Samaniego JL, Castañón-González JA, Buhse T (2014a) Polar profile of antiviral peptides from AVPpred database. Cell Biochem Biophys 70: 1469-1477.
  • Polanco C, Samaniego JL, Castañón-González JA, Buhse T, Sordo ML (2013a) Characterization of a possible uptake mechanism of selective antibacterial peptides. Acta Biochim Pol 60: 629-633.
  • Polanco C, Samaniego-Mendoza JL, Buhse T, Castañón-González JA, Leopold-Sordo M (2014b) Polar characterization of antifungal peptides from APD2 database. Cell Biochem Biophys 70: 1479-1488.
  • Polanco C, Castañón-González JA, Uversky VM Comment to: Buhimschi IA, Nayeri UA, Zhao G, Shook LL, Pensalfini A, Funai EF, Bernstein IM, Glabe CG, Buhimschi CS (2014e) Protein misfolding, congophilia, oligomerization, and defective amyloid processing in preeclampsia. Sci Transl Med 6: 245ra92.
  • Polanco C, Samaniego-Mendoza JL, Castañón-González JA, Buhse T Comment to: Howard SJ, Hopwood S, Davies SC. (2014d) Antimicrobial resistance: a global challenge. Sci Transl Med
  • Schmidt MA, Riley LW, Benz I (2003) Sweet new world: glycoproteins in bacterial pathogens. Trends Microbiol 11: 554-561.
  • UN Millennium Project 2005 (2005) Investing in strategies to reverse the global incidence of TB. Task Force on HIV/AIDS, Malaria, TB, and Access to Essential Medicines. Available at:
  • Upreti RK, Kumar M, Shankar V (2003) Bacterial glycoproteins: functions, biosynthesis and applications. Proteomics 3: 363-379.
  • Wang G, Li X, Wang Z (2009) APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res 37: D933−D937.
  • World Health Organization (WHO) (2014)

Document Type

Publication order reference

Identifiers

YADDA identifier

bwmeta1.element.bwnjournal-article-abpv62p191kz
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.