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Titolo:
Growth inhibition of Bacteroides fragilis by hemopexin: proteolytic degradation of hemopexin to overcome heme limitation
Autore:
Rocha, ER; Smith, A; Smith, CJ; Brock, JH;
Indirizzi:
E Carolina Univ, Sch Med, Dept Microbiol & Immunol, Greenville, NC 27858 USA E Carolina Univ Greenville NC USA 27858 Immunol, Greenville, NC 27858 USA Univ Missouri, Sch Biol Sci, Div Mol Biol & Biochem, Kansas City, MO 64110USA Univ Missouri Kansas City MO USA 64110 Biochem, Kansas City, MO 64110USA Western Infirm, Dept Immunol, Glasgow G11 6NT, Lanark, Scotland Western Infirm Glasgow Lanark Scotland G11 6NT G11 6NT, Lanark, Scotland
Titolo Testata:
FEMS MICROBIOLOGY LETTERS
fascicolo: 1, volume: 199, anno: 2001,
pagine: 73 - 78
SICI:
0378-1097(20010515)199:1<73:GIOBFB>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
HAEMOPHILUS-INFLUENZAE; EXOCELLULAR PROTEASE; HEMOGLOBIN RECEPTOR; VIBRIO-VULNIFICUS; BINDING PROTEINS; BOUND IRON; TRANSFERRIN; EXPRESSION; TRANSPORT; HAPTOGLOBIN;
Keywords:
heme; hemopexin; heme-binding protein; protease; Bacteroides fragilis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Rocha, ER E Carolina Univ, Sch Med, Dept Microbiol & Immunol, Greenville, NC 27858 USA E Carolina Univ Greenville NC USA 27858 reenville, NC 27858 USA
Citazione:
E.R. Rocha et al., "Growth inhibition of Bacteroides fragilis by hemopexin: proteolytic degradation of hemopexin to overcome heme limitation", FEMS MICROB, 199(1), 2001, pp. 73-78

Abstract

The stimulatory effect of heme on growth of Bacteroides fragilis. an anaerobic human pathogen. was strongly inhibited by hemopexin, an avid (K-d < 1 pM) heme-binding plasma protein. Both rabbit and human hemopexins were bacteriostatic for a limited period of time, suggesting an adaptation by B. fragilis to heme-limited growth, and that hemopexin-bound heme can eventually be utilized by the bacteria. The inhibitory effect of hemopexin was lost when heme in the medium was replaced by protoporphyrin IX, which is bound less strongly by hemopexin (Kd similar to1 muM). Protease activity was detected in the culture supernatant of B. fragilis grown in the presence of heme plus hemopexin but not in the presence of free heme, protoporphyrin IX or protoporphyrin IX plus hemopexin. suggesting that the enzyme(s) is induced byheme macrocycle limitation due to the scavenging effect of hemopexin. Thisprotease activity uas able to degrade rabbit hemopexin and human hemopexin, as well as human transferrin and ovalbumin. and may be a due to a serine protease since it was inhibited by phenylmethylsulfonyl fluoride (PMSF) butnot by EDTA, leupeptin, pepstatin A or aprotinin. Thus. B. fragilis may overcome hemopexin-mediated heme limitation by secreting inducible protease(s), shown here to make protein-bound heme available to the microorganism. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 18:21:10