1887

Abstract

Attacin is a 20 kDa antibacterial protein, originally isolated from the immune haemolymph of . It has been demonstrated previously that attacin causes increased permeability of the outer membrane of and inhibition of outer-membrane protein synthesis at the transcriptional level. This is accompanied by inhibition of growth. Here, LPS is shown to serve as the receptor for attacin and evidence is presented that attacin does not need to enter the cell to exert its activity. The increase in outer-membrane permeability precedes any increase in inner-membrane permeability by at least one generation time (∼ 45 min), and the inhibiting effect of attacin on synthesis of outer-membrane proteins is detectable after only 10 min. It is also shown that attacin causes induction of several stress proteins and increased synthesis of LPS within, respectively, 25 and 60 min of treatment. Based on the results presented, it is proposed that attacin has the unique ability to specifically interfere with synthesis of outer-membrane proteins without entering the inner membrane or cytoplasm.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-144-8-2179
1998-08-01
2019-11-12
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-144-8-2179
Loading
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error