Analysis of a cloned sequence of Legionella pneumophila encoding a 38 kD metalloprotease possessing haemolytic and cytotoxic activities.

Abstract:

:The DNA encoding the zinc metalloprotease of Legionella pneumophila Philadelphia 1 has been isolated and expressed in Escherichia coli. This protein, which is 38,000 Daltons in size, possesses immunological and biochemical properties identical to those previously described for the purified L. pneumophila protease. Periplasmic extracts of E. coli clones expressing the recombinant protease are also capable of causing the haemolysis of canine erythrocytes and the cytotoxic destruction of CHO cells. Using transposon mutagenesis, it was determined that a maximum of 1.2 kb of DNA encoded all three biological activities. Inactivation of proteolytic activity by transposon insertion occurred concomitantly with losses of the haemolytic and cytotoxic phenotypes. A putative regulatory sequence approximately 200-500 bp upstream of the gene's coding region was identified. A 4.0 kb fragment encoding these activities hybridized to the chromosomal DNA of the parent strain of L. pneumophila Philadelphia 1 as well as clinical isolates of L. pneumophila.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Quinn FD,Tompkins LS

doi

10.1111/j.1365-2958.1989.tb00228.x

subject

Has Abstract

pub_date

1989-06-01 00:00:00

pages

797-805

issue

6

eissn

0950-382X

issn

1365-2958

journal_volume

3

pub_type

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