Antibody structural variation in rainbow trout fluids

被引:28
作者
Bromage, ES [1 ]
Ye, JM [1 ]
Kaattari, SL [1 ]
机构
[1] Virginia Inst Marine Sci, Coll William & Mary, Dept Environm & Aquat Anim Hlth, Gloucester Point, VA 23062 USA
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 2006年 / 143卷 / 01期
关键词
rainbow trout; antibody; redox forms; mucus; ovarian fluid; eggs; titer; structure; regional immunity;
D O I
10.1016/j.cbpb.2005.10.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Rainbow trout (Oncorhynchus mykiss) were immunized with tiinitroplienylated-keyhole limpet hemocyanin (TNP-KLH) and the redox structure of induced anti-TNP antibodies from the serum, mucus, egg and ovarian fluid was examined. In conducting these studies it was determined that all TNP-specific antibody from each source possessed the mAb-specific H chain (1 - 14) epitopes, which facilitated the direct structural analysis of the induced antibodies. A protocol was developed which ensured complete adsorption of all specific anti-TNP antibody from each fluid. Together these protocols permitted the unbiased compositional analysis of all redox forms of the anti-TNP antibodies from each source. All antibodies, regardless of source, possessed the same molecular mass, characteristic of the trout tetramer (800 kDa). It was found that specific antibody titers were significantly higher in male than female trout, while the degree of disulfide polymerization was relatively invariant in male antibodies, while being highly variable in female antibodies. Within the females, no distinctively different redox ratios were between antibodies isolated from sera, ovarian fluid or eggs: however, mucus antibodies possessed a unique redox structure consisting of halfmeric constituents that were not observed in antibodies from other fluids. (c) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码:61 / 69
页数:9
相关论文
共 43 条
[1]  
ARKOOSH MR, 1990, SOS PUBLICATIONS, P15
[2]   Use of staphylococcal protein A in the analysis of teleost immunoglobulin structural diversity [J].
Bromage, ES ;
Ye, JM ;
Owens, L ;
Kaattari, IM ;
Kaattari, SL .
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY, 2004, 28 (7-8) :803-814
[3]   Antibody-antigen kinetics following immunization of rainbow trout (Oncorhynchus mykiss) with a T-cell dependent antigen [J].
Cain, KD ;
Jones, DR ;
Raison, RL .
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY, 2002, 26 (02) :181-190
[4]   Alterations in total protein, IgM and specific antibody activity of male and female sea bass (Dicentrarchus labrax L, 1758) sera following injection with killed Vibrio anguillarum [J].
Coeurdacier, JL ;
Pepin, JF ;
Fauvel, C ;
Legall, P ;
Bourmaud, AF ;
Romestand, B .
FISH & SHELLFISH IMMUNOLOGY, 1997, 7 (03) :151-160
[5]   Trout ovulatory proteins are partially responsible for the anti-proteolytic activity found in trout coelomic fluid [J].
Coffman, MA ;
Goetz, FW .
BIOLOGY OF REPRODUCTION, 1998, 59 (03) :497-502
[6]  
Corthesy B, 1999, CURR TOP MICROBIOL, V236, P93
[7]   The immunoglobulin heavy-chain locus in zebrafish: identification and expression of a previously unknown isotype, immunoglobulin Z [J].
Danilova, N ;
Bussmann, J ;
Jekosch, K ;
Steiner, LA .
NATURE IMMUNOLOGY, 2005, 6 (03) :295-302
[8]   LYMPHOCYTE HETEROGENEITY IN THE TROUT, SALMO-GAIRDNERI, DEFINED WITH MONOCLONAL-ANTIBODIES TO IGM [J].
DELUCA, D ;
WILSON, M ;
WARR, GW .
EUROPEAN JOURNAL OF IMMUNOLOGY, 1983, 13 (07) :546-551
[9]   STUDIES ON CONTROL OF IGM ANTIBODY-SYNTHESIS .3. PREFERENTIAL FORMATION OF ANTI-DNP-ANTIBODIES OF HIGH FUNCTIONAL AFFINITY IN COURSE OF IMMUNE-RESPONSE IN CARP [J].
FIEBIG, H ;
GRUHN, R ;
AMBROSIUS, H .
IMMUNOCHEMISTRY, 1977, 14 (11-1) :721-726
[10]  
FRANKLIN EC, 1975, ACTA ENDOCRINOL-COP, V78, P77