Rapid screening test for tuberculosis using a 38-kDa antigen fromMycobacterium tuberculosis

Rosales-Borjas, Disney M.; Zambrano-Villa, Sergio; Elinos, Martha; Kasem, Harum; Osuna, Antonio; Mancilla, Raúl; Ortiz‐Ortiz, Librado

doi:10.1002/(sici)1098-2825(1998)12:2<126::aid-jcla9>3.0.co;2-8

Cited by 5 publications

(4 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The screening test for tuberculosis using 38 kDa antigens is highly specific, easy to handle and requires no equipment. Therefore, such ELISA is particularly useful for field studies (Rosales‐Borjas et al , 1998). Sera from sheep infected and immunized with Mycobacterium para tuberculosis are found to have antibodies to 38 kDa mycobacterial antigen (Valentin‐Weigand & Moriarty, 1992).…”

Section: Antigen 60 (A60)mentioning

confidence: 99%

Retracted: Antibodies to mycobacterial antigens for diagnosis of tuberculosis

Verma

Jain

2007

FEMS Immunology &Amp; Medical Microbiology

View full text Add to dashboard Cite

In spite of the advent of several newer modalities in molecular and immunological methods of diagnosis, the diagnosis of smear negative tuberculosis is a major problem even today. Use of antibody detection ELISA for the purpose has been evaluated by many authors using a variety of antigens derived from mycobacteria. These antigens are reported to have many advantages and disadvantages. Here we review commonly used antigens used for detection of antimycobacterial antibodies for diagnosis of tuberculosis. Each antigen is reviewed for its application in diagnosis, sensitivity, specificity, cross-reactivity and clinical application.

show abstract

Section: Antigen 60 (A60)mentioning

confidence: 99%

Retracted: Antibodies to mycobacterial antigens for diagnosis of tuberculosis

Verma

Jain

2007

FEMS Immunology &Amp; Medical Microbiology

View full text Add to dashboard Cite

show abstract

“…Recently designed strip tests, based on immunochromatographic method, which enable quick detection of rod‐shaped bacilli antibodies in serum, may help. Wilkinson and Ivanyi (12, 13) report that the percentage of positive results in serological tests based on an immunoenzymatic method using a 38 kDa antigen in patients with non‐pulmonary tuberculosis was 70–80%, irrespective of the affected organ. An histopathological examination is necessary for the final diagnosis.…”

Section: Discussionmentioning

confidence: 99%

Acute isolated tuberculous appendicitis

Wyrobiec

Sandelewski²,

Głowacka

et al. 2006

J Clin Pharm Ther

View full text Add to dashboard Cite

Non-pulmonary tuberculosis is found with different frequencies in different countries of the world. It is said to constitute about 4% of all tuberculosis cases in Poland, about 25% in England and Wales and about 17% in the USA. It seems that these differences are the result of differences in rates of diagnosis and registration of new tuberculosis cases. This in turn is influenced by public health funding in the individual countries. In this work, we present a case of acute, isolated, tuberculous inflammation of the appendix. We call attention to the fact that pre-operative diagnosis is practically impossible. Clinical symptoms do not point to inflammatory changes. Only surgical evaluation, and especially the result of histopathological examination make it to possible to establish the final diagnosis to initiation of anti-tuberculous treatment.

show abstract

“…For the reasons that ProGlycProt has a broad taxonomic coverage ( Supplementary Figure S1 ) and published evidence of glycosylation for all entries, it provides an updated and realistic estimate of the extent of occurrence of protein glycosylation in prokaryotes. To serve a broader interest in prokaryotic glycoproteins, OSTs and associated GTs for their potential applied and basic applications ( 1–5 , 35 ), the database provides a variety of biologically and experimentally relevant information ( Supplementary Table S1 and S2 ) about both native and glyco-engineered proteins of prokaryotes in addition to their cataloguing. Existing entries are updated in real time as soon as relevant literature is published or obtained.…”

Section: Current Scope and Future Perspectivementioning

confidence: 99%

“…Protein glycosylation in prokaryotes is a recent but rapidly growing area of research. An expanding repertoire of prokaryotic glycoproteins is increasingly being explored as a target for therapeutic interventions in diagnostics ( 1 ), vaccines ( 2 ), as future nano-machines using proteins like S layer glycoproteins ( 3 ) and as a strategy to improve industrially important enzymes for specific attributes ( 4 , 5 ).…”

Section: Introductionmentioning

confidence: 99%

ProGlycProt: a repository of experimentally characterized prokaryotic glycoproteins

Bhat¹,

Mondal²,

Chauhan³

et al. 2011

Nucleic Acids Research

View full text Add to dashboard Cite

ProGlycProt (http://www.proglycprot.org/) is an open access, manually curated, comprehensive repository of bacterial and archaeal glycoproteins with at least one experimentally validated glycosite (glycosylated residue). To facilitate maximum information at one point, the database is arranged under two sections: (i) ProCGP—the main data section consisting of 95 entries with experimentally characterized glycosites and (ii) ProUGP—a supplementary data section containing 245 entries with experimentally identified glycosylation but uncharacterized glycosites. Every entry in the database is fully cross-referenced and enriched with available published information about source organism, coding gene, protein, glycosites, glycosylation type, attached glycan, associated oligosaccharyl/glycosyl transferases (OSTs/GTs), supporting references, and applicable additional information. Interestingly, ProGlycProt contains as many as 174 entries for which information is unavailable or the characterized glycosites are unannotated in Swiss-Prot release 2011_07. The website supports a dedicated structure gallery of homology models and crystal structures of characterized glycoproteins in addition to two new tools developed in view of emerging information about prokaryotic sequons (conserved sequences of amino acids around glycosites) that are never or rarely seen in eukaryotic glycoproteins. ProGlycProt provides an extensive compilation of experimentally identified glycosites (334) and glycoproteins (340) of prokaryotes that could serve as an information resource for research and technology applications in glycobiology.

show abstract

Rapid screening test for tuberculosis using a 38-kDa antigen fromMycobacterium tuberculosis

Cited by 5 publications

References 16 publications

Retracted: Antibodies to mycobacterial antigens for diagnosis of tuberculosis

Retracted: Antibodies to mycobacterial antigens for diagnosis of tuberculosis

Acute isolated tuberculous appendicitis

ProGlycProt: a repository of experimentally characterized prokaryotic glycoproteins

Contact Info

Product

Resources

About