Characterization of the Legionella pneumophila DnaJ-Like Protein DjlA: Virulence Attenuation of djlA Mutants

Legionella ◽  
2014 ◽  
pp. 64-67
Author(s):  
Werner Brabetz ◽  
Helmut Brade ◽  
Matthias Frosch ◽  
Edeltraud Lüneberg
1995 ◽  
Vol 115 (1) ◽  
pp. 71-78 ◽  
Author(s):  
J. H. Helbig ◽  
P. C. Lück ◽  
Y. A. Knirel ◽  
W. Witzleb ◽  
U. Zähringer

SummaryFor identification of lipopolysaccharide (LPS)-associated epitopes ofLegionella pneumophilaserogroup 1, LPS of strain Philadelphia 1 was investigated using monoclonal antibodies (MAbs). The O-specific chain of LPS is a homopolymer of 5-acetamidino-7-acetamido-8-O-acetyl-3,5,7,9-tetradeoxy-D-glycero-L-galacto-nonulosonic acid. At least four immunoaccessible epitopes were recognized by different MAbs on the intact LPS. AfterO-deacetylation of LPS, the reactivity of one of the MAbs (MAb 3/1) was lost, indicating thus that the corresponding epitope is associated with the 8-O-acetyl group. Since the reactivity pattern of the MAb 3/1 is identical with those of the MAb 2 which was considered as a virulence marker for serogroup 1, this epitope may be involved in mediating virulence inL. pneumophila. Four MAbs specific to strains of serogroup 1 other than the monoclonal subtype Philadelphia recognized epitopes on theO-deacetylated LPS of strain Philadelphia 1 and, therefore, the virulence-associated epitope blocks recognition of the immunodeterminants that are accessible on the intact LPS of the strains lacking this epitope.


1983 ◽  
Vol 17 (2) ◽  
pp. 346-348 ◽  
Author(s):  
W F Bibb ◽  
P M Arnow ◽  
D L Dellinger ◽  
S R Perryman

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