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Infect Immun, August 1998, p. 3974-3977, Vol. 66, No. 8
National Institute of Cholera and Enteric
Diseases, Calcutta, India
Received 26 February 1998/Returned for modification 3 April
1998/Accepted 8 May 1998
Two hybrid clones producing monoclonal antibodies (MAbs) raised
against the purified enterotoxic hemolysin-phospholipase C (HlyPC)
bifunctional molecule of a Vibrio cholerae O139 strain were
used to study its enterotoxicity in relation to its hemolytic and
enzymatic activities. Fab fragments of MAbs from ascites
produced by the two hybrids neutralized the hemolytic activity of
HlyPC, leaving the enzymatic activity unaffected. In ligated rabbit
ileal loop and infant mouse intestine, the Fab fragments of the MAbs were not able to neutralize the enterotoxicity of HlyPC,
suggesting that PC rather than Hly is the enterotoxic moiety of
the molecule. The enterotoxicity of the purified PC molecule
isolated from an Hly
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Use of Monoclonal Antibodies To Identify
Phospholipase C as the Enterotoxic Factor of the Bifunctional
Hemolysin-Phospholipase C Molecule of Vibrio cholerae
O139
spontaneous mutant of the
HlyPC-producing parent strain further confirms this contention. The
Hly molecule isolated from a PC
mutant was not
diarrheagenic.
*
Corresponding author. Mailing address: National
Institute of Cholera and Enteric Diseases, Department of
Biochemistry, P-33, C.I.T. Rd., Scheme XM, Beliaghata, Calcutta 700 010, India. Phone: 91(033) 350 4598. Fax: 91(033) 350 5066. E-mail:
icmrnicd{at}ren.nic.in.
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