Isolation of a 33-kDa protein antigen from delipidified Mycobacterium tuberculosis H37Rv.

Abstract:

:A 33-kDa protein (TB33) was isolated from a delipidated cell sonicate (CS) of Mycobacterium tuberculosis H37Rv (grown in Middlebrook 7H9 broth supplemented with glucose) using immobilized metal affinity chromatography (IMAC) on a nickel-nitrilotriacetic acid (Ni-NTA) column. TB33 could not be isolated from the culture filtrate (CF) of M. tuberculosis H37Rv using Ni-NTA. TB33 was recognized by monoclonal antibodies (mAb) known to react with proteins of M. tuberculosis with a molecular mass of 33/34 kDa; namely, mAb F126-5, F67-1 and F126-2. The N-terminal amino acid sequence of TB33 was found to be Xaa-Xaa-Thr-Pro-Ala-Asp-Val-Ser/Cys-Asn-Val-Ala-Ile and thus, shows identity with the N-terminal of antigen 84 of M. tuberculosis except for two mismatches. Antibodies to TB33 could be raised in mice by administering four injections of TB33 (40 micrograms total protein). Sera from tuberculosis patients reacted with TB33, while those from normal healthy individuals did not.

journal_name

Med Microbiol Immunol

authors

Deshpande RG,Khan MB,Bhat DA,Navalkar RG

doi

10.1007/s004300050025

subject

Has Abstract

pub_date

1996-11-01 00:00:00

pages

153-5

issue

3

eissn

0300-8584

issn

1432-1831

journal_volume

185

pub_type

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