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Titolo:
The cell envelope-bound metalloprotease (camelysin) from Bacillus cereus is a possible pathogenic factor
Autore:
Fricke, B; Drossler, K; Willhardt, I; Schierhorn, A; Menge, S; Rucknagel, P;
Indirizzi:
Univ Halle Wittenberg, Fac Med, Inst Physiol Chem, D-06097 Halle Saale, Saale, Germany Univ Halle Wittenberg Halle Saale Saale Germany D-06097 e, Saale, Germany Univ Halle Wittenberg, Fac Life Sci, Inst Biochem, Halle Saale, Saale, Germany Univ Halle Wittenberg Halle Saale Saale Germany le Saale, Saale, Germany Max Planck Res Unit, Halle Saale, Saale, Germany Max Planck Res Unit Halle Saale Saale Germany alle Saale, Saale, Germany
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
fascicolo: 2, volume: 1537, anno: 2001,
pagine: 132 - 146
SICI:
0925-4439(20010928)1537:2<132:TCEM(F>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
CLOSTRIDIUM-HISTOLYTICUM COLLAGENASE; BACTEROIDES-FRAGILIS; MICROBIAL PROTEINASES; PARACELLULAR BARRIER; MEMBRANE-PROTEINS; EPITHELIAL-CELLS; PURIFICATION; SPECIFICITY; PROTEASE; SUBSTRATE;
Keywords:
membrane protease; solubilization; purification; characterization; metalloprotease; collagenase; cleavage specificity; substrate specificity; fibrinogenolysis; fibrinolysis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Fricke, B Univ Halle Wittenberg, Fac Med, Inst Physiol Chem, D-06097 HalleSaale, Saale, Germany Univ Halle Wittenberg Halle Saale Saale Germany D-06097 Germany
Citazione:
B. Fricke et al., "The cell envelope-bound metalloprotease (camelysin) from Bacillus cereus is a possible pathogenic factor", BBA-MOL BAS, 1537(2), 2001, pp. 132-146

Abstract

A novel membrane proteinase of the nosocomial important bacteria species Bacillus cereus (synonyms: camelysin, CCMP) was purified up to homogeneity as was shown by mass spectrometry in its amphiphilic form. Camelysin is a neutral metalloprotease with a molecular mass of 19 kDa. Its unique N-terminus Phe-Phe-Ser-Asp-Lys-Glu-Val-Ser-Asn-Asn-Thr-Phe-Ala-Ala-Gly-Thr-Leu-Asp-Leu-Thr-Leu-Asn-Pro-Lys-Thr-Leu-Val-Asp-(Ile-Lys-Asp)- was not detected in the protein data bases during BLAST searches, but in the partially sequencedgenome of Bacillus anthracis, coding for an unknown protein. Cleavage sites of the membrane proteinase for the insulin A- and B-chains were determined by mass spectrometry and N-terminal sequencing. Camelysin prefers cleavage sites in front of aliphatic and hydrophilic amino acid residues (-OH, -SO3H, amido group), avoiding bulky aromatic residues. The internally quenchedfluorogenic substrates of the matrix metalloproteases 2 and 7 were cleavedwith the highest efficiency at the Leu- down arrow -Gly or Leu- down arrow-Ala bond with the smaller residue in the P-1' position. The protein specificity is broad - all various kinds of casein were cleaved as well as acid-soluble collagen, globin and ovalbumin; intact insulin was destroyed only to a low extent. Actin, collagen type I, fibrinogen, fibrin, alpha (2)-antiplasmin and alpha (1)-antitrypsin were cleaved. The protease formed SDS-stable complexes with Glu-plasminogen and antithrombin III, visible after SDS electrophoresis by gold staining and Western blot. The CCMP-plasminogen complex caused a partial activation of plasminogen to plasmin. Camelysin interacts with proteins of the blood coagulation cascade and could facilitate thepenetration of fibrin clots and of the extracellular matrix during bacterial invasion. (C) 2001 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 07/04/20 alle ore 23:16:47