Previous Article | Next Article ![]()
Infection and Immunity, February 2000, p. 801-808, Vol. 68, No. 2
National Veterinary
Institute1 and Institute of Immunology
(IGRI), The National Hospital,2 Oslo, Norway
Received 26 July 1999/Returned for modification 22 September
1999/Accepted 11 November 1999
Antigens characteristic for Mycobacterium avium
subspecies paratuberculosis were identified by crossed
immunoelectrophoresis (CIE) and by absorbing out cross-reactive
antigens by using a polyclonal and polyvalent Mycobacterium
avium subspecies avium antiserum. Two antigens were
present in M. avium subsp. paratuberculosis and
not detected in Mycobacterium avium subsp.
avium. They were identified as antigens 17 and 20 in a CIE
reference system for M. avium subsp.
paratuberculosis antigens. Purified antigen 20 was
identified as alkyl hydroperoxide reductase C (AhpC) while the
N-terminal part of purified antigen 17 showed 80% homology with alkyl
hydroperoxide reductase D (AhpD) of Mycobacterium
tuberculosis. AhpC had a nonreduced mobility in sodium dodecyl
sulfate-polyacrylamide gel electrophoresis corresponding to a molecular
mass of 45 kDa and is probably a homodimer linked with disulfide
bridges in its native form. AhpD had a mobility corresponding to 19 kDa. Monospecific rabbit antiserum against AhpC and AhpD reacted with 9 strains of M. avium subsp. paratuberculosis but
not with 20 other mycobacterial strains except for a
Mycobacterium gordonae strain, against which a weak
cross-reactive band was produced. Goats experimentally infected with
M. avium subsp. paratuberculosis had strong
gamma interferon (IFN-
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Alkyl Hydroperoxide Reductases C and D Are Major
Antigens Constitutively Expressed by Mycobacterium avium
subsp. paratuberculosis
) responses toward both AhpC and AhpD, and
they also had antibodies against AhpC. The ability of AhpC and AhpD to
induce IFN-
production shows that these proteins potentially could
be used in future vaccines or in diagnostic assays. These results
further show that AhpC and AhpD are immunologically important proteins
which are constitutively and highly expressed in M. avium subsp. paratuberculosis without the bacteria being
submitted to oxidative stress and that the specificities of antigens
can be a matter of different levels of protein expression in various species as well as distinct structural differences.
*
Corresponding author. Mailing address: Section of
Immunoprophylaxis, National Veterinary Institute, P.O. Box 8156, Dep.
0033, Oslo, Norway. Phone: 47 22 96 46 34. Fax: 47 22 46 88 90. E-mail: Ingrid.Olsen{at}vetinst.no.
Present address: National Institute of Public Health, Department of
Environmental Medicine, Oslo, Norway.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»