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Titolo:
IRON ACQUISITION BY MYCOBACTERIUM-TUBERCULOSIS - ISOLATION AND CHARACTERIZATION OF A FAMILY OF IRON-BINDING EXOCHELINS
Autore:
GOBIN J; MOORE CH; REEVE JR; WONG DK; GIBSON BW; HORWITZ MA;
Indirizzi:
UNIV CALIF LOS ANGELES,SCH MED,DEPT MED LOS ANGELES CA 90095 UNIV CALIF SAN FRANCISCO,DEPT CHEM & PHARMACEUT CHEM SAN FRANCISCO CA94143
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 11, volume: 92, anno: 1995,
pagine: 5189 - 5193
SICI:
0027-8424(1995)92:11<5189:IABM-I>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTERFERON-GAMMA; INTRACELLULAR MULTIPLICATION; LEGIONELLA-PNEUMOPHILA; TRANSFERRIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
17
Recensione:
Indirizzi per estratti:
Citazione:
J. Gobin et al., "IRON ACQUISITION BY MYCOBACTERIUM-TUBERCULOSIS - ISOLATION AND CHARACTERIZATION OF A FAMILY OF IRON-BINDING EXOCHELINS", Proceedings of the National Academy of Sciences of the United Statesof America, 92(11), 1995, pp. 5189-5193

Abstract

Mycobacterium tuberculosis, the primary agent of tuberculosis, must acquire iron from the host to cause infection. To do so, it releases high-affinity iron-binding siderophores called exochelins. Exochelins are thought to transfer iron to another type of high-affinity iron-binding molecule in the bacterial cell wall, mycobactins, for subsequent utilization by the bacterium, In this paper, we describe the purification of exochelins of M. tuberculosis and their characterization by mass spectrometry, Exochelins comprise a family of molecules whose most abundant species range in mass from 744 to 800 Ha in the neutral Fe3+-loaded state. The molecules form two 14-Da-increment series, one saturated and the other unsaturated, with the increments reflecting different numbers of CH2 groups on a side chain, These series further subdivide into serine- or threonine-containing species. The virulent M. tuberculosis Erdman strain and the avirulent M. tuberculosis H37Ra strain produce a similar set of exochelins. Based on a comparison of their tandemmass spectra, exochelins share a common core structure with mycobactins. However, exochelins are smaller than mycobactins due to a shorter alkyl side chain, and the side chain of exochelins terminates in a methyl ester, These differences render exochelins more polar than the lipophilic mycobactins and hence soluble in the aqueous extracellular milieu of the bacterium in which they bind iron in the host.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 12:53:09