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(Received for publication, September 15, 1997)
From the Actinobacillus
actinomycetemcomitans leukotoxin and Escherichia coli
Volume 272, Number 48,
Issue of November 28, 1997
pp. 30463-30469
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
RTX Toxins Recognize a
2 Integrin on the Surface of Human
Target Cells
,
,
,
,
,
,
,
,
and
Leon Levy Research Center for Oral Biology,
University of Pennsylvania, Philadelphia, Pennsylvania 19104-6002, the ¶ First Department of Oral Surgery, School of Dental Medicine
University of Ohu, 31-1, Aza-Misumido, Tomita-cho, Koriyama-shi,
Fukushima, 963, Japan, and 
Celltech Ltd., Slough
SL1 4EN, United Kingdom
-hemolysin are RTX toxins that kill human immune cells. We have
obtained a monoclonal antibody (295) to a cell surface molecule present
on toxin-sensitive HL60 cells that can inhibit cytolysis by both RTX
toxins. Utilization of this monoclonal antibody for immunoaffinity
purification of detergent-solubilized target cell membranes yielded two
polypeptide chains of approximate molecular masses of 100 and 170 kDa.
Microsequencing of tryptic peptides from the two proteins showed
complete homology with CD11a and CD18, the two subunits of the 
2
integrin, lymphocyte function-associated antigen 1 (LFA-1). Anti-CD11a
and CD18 monoclonal antibodies also inhibited RTX toxin-mediated
cytolysis. Direct binding experiments demonstrated the ability of an
immobilized RTX to bind LFA-1 heterodimers present in a detergent
lysate of human HL60 target cells. Transfection of CD11a and CD18
integrin genes into a cell line (K562) that is not sensitive to either
RTX toxin resulted in LFA-1 expressing cells, KL/4, that were sensitive
to both toxins. These experiments identify LFA-1 as a cell surface
receptor that mediates toxicity of members of this family of
pore-forming toxins.
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