Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Mycobacterial protein HbhA binds human complement component C3
Autore:
Mueller-Ortiz, SL; Wanger, AR; Norris, SJ;
Indirizzi:
Univ Texas, Sch Med, Dept Pathol & Lab Med, Hlth Sci Ctr, Houston, TX 77225 USA Univ Texas Houston TX USA 77225 Med, Hlth Sci Ctr, Houston, TX 77225 USA Univ Texas, Sch Med, Grad Sch Biomed Sci, Hlth Sci Ctr, Houston, TX 77225 USA Univ Texas Houston TX USA 77225 Sci, Hlth Sci Ctr, Houston, TX 77225 USA
Titolo Testata:
INFECTION AND IMMUNITY
fascicolo: 12, volume: 69, anno: 2001,
pagine: 7501 - 7511
SICI:
0019-9567(200112)69:12<7501:MPHBHC>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-MONOCYTES; ALVEOLAR MACROPHAGES; 45-KILODALTON GLYCOPROTEIN; MOLECULAR CHARACTERIZATION; MEDIATES PHAGOCYTOSIS; NONOPSONIC BINDING; OUTER-MEMBRANE; AVIUM COMPLEX; TUBERCULOSIS; RECEPTORS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Norris, SJ Univ Texas, Sch Med, Dept Pathol & Lab Med, Hlth Sci Ctr, POB 20708, Houston, TX 77225 USA Univ Texas POB 20708 Houston TX USA 77225 Houston, TX 77225 USA
Citazione:
S.L. Mueller-Ortiz et al., "Mycobacterial protein HbhA binds human complement component C3", INFEC IMMUN, 69(12), 2001, pp. 7501-7511

Abstract

Mycobacterium tuberculosis and Mycobacterium avium are facultative intracellular pathogens that are able to survive and replicate in mononuclear phagocytes. Human complement component C3 has previously been shown to mediate attachment and phagocytosis of these bacteria by mononuclear phagocytes. Inthis study, a C3 ligand affinity blot protocol was used to identify a 30-kDa C3-binding protein in M. tuberculosis and Mycobacterium smegmatis and a 31-kDa C3-binding protein in M. avium. The C3-binding proteins in M. tuberculosis and M. avium localized to the cell membrane fraction and partitionedto the detergent fraction during Triton X-114 phase partitioning. The C3-binding protein from M. tuberculosis was partially purified using a cation exchange column and was shown to bind concanavalin A. The N terminus and an internal fragment of the partially purified C3-binding protein were subjected to amino acid sequence analysis. The resulting amino acid sequences matched the Al. tuberculosis heparin-binding hemagglutinin (HbhA) protein. Recombinant full-length HbhA and the C terminus of HbhA fused to maltose-binding protein, but not recombinant HbhA lacking the C-terminal region, bound human C3. Recombinant full-length HbhA coated on polystyrene beads, was foundto enhance the adherence and/or phagocytosis of the coated beads to J774.A1 cells in both the presence and absence of human serum. The presence of complement-sufficient serum increased the adherence of the HbhA-coated beads to the J774.A1 cells in a C3-dependent manner. If HbhA within the bacterialcell membrane functions similarly to isolated HbhA, this protein may enhance the adherence and phagocytosis of Al. tuberculosis and M. avium to mononuclear phagocytes through the binding of C3 and interaction with C3 receptors on mononuclear phagocytes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 15:45:49