Sequences in antibody molecules important forreceptor-mediated transport into the chicken egg yolk

被引:68
作者
Morrison, SL
Mohammed, MS
Wims, LA
Trinh, R
Etches, R
机构
[1] Univ Calif Los Angeles, Inst Mol Biol, Dept Microbiol Immunol & Mol Genet, Los Angeles, CA 90095 USA
[2] Univ Guelph, Dept Anim & Poultry Sci, Guelph, ON N1G 2W1, Canada
关键词
immunoglobulin transport; chicken egg yolk; antibodies;
D O I
10.1016/S0161-5890(01)00095-5
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
Large quantities of antibodies are transported into the yolk of the chicken's egg. We have identified several regions within the antibody molecule important for its uptake into the egg yolk. An intact Fc and hinge region but not the Fc-associated carbohydrate are required for transport. Our data suggest that the C(H)2/C(H)3 interface is recognized by the receptor responsible for immunoglobulin (Ig) transport. At this interface, residues 251-254 form an exposed loop on the surface Of C(H)2. Chicken IgY (cIgY) hits the sequence LYIS and human IgG (hIgG) has the sequence LMIS at these positions; mutation of MIS to glycines results in an IgG that is not transported. A second site important for transport is at positions 429-432 within C(H)3. All transported antibodies have the sequence HEAL, whereas, murine IgG2b (mIgG2b) with the sequence HEGL and cIgA with the sequence HDGI fail to be transported. hIgA has the HEAL sequence and is transported. (C) 2002 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:619 / 625
页数:7
相关论文
共 47 条
[1]   MONOCLONAL IGM RHEUMATOID FACTORS BIND IGG AT A DISCONTINUOUS EPITOPE COMPRISED OF AMINO-ACID LOOPS FROM HEAVY-CHAIN CONSTANT-REGION DOMAIN-2 AND DOMAIN-3 [J].
ARTANDI, SE ;
CALAME, KL ;
MORRISON, SL ;
BONAGURA, VR .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (01) :94-98
[2]   CRYSTALLOGRAPHIC STUDIES OF IMMUNOGLOBULINS - CRYSTALLIZATION OF THE FC FRAGMENT OF RABBIT IGG WITH AND WITHOUT CLEAVAGE OF THE INTER-CHAIN DISULFIDE BRIDGE [J].
ASCHAFFENBURG, R ;
LEWIS, M ;
PHILLIPS, DC ;
PRESS, EM ;
SMITH, SG ;
SUTTON, BJ ;
MOUNTFORD, CW .
JOURNAL OF MOLECULAR BIOLOGY, 1979, 135 (04) :1033-1036
[3]   STRUCTURE AND FUNCTION OF CONSTANT REGIONS OF IMMUNOGLOBULINS [J].
BEALE, D ;
FEINSTEIN, A .
QUARTERLY REVIEWS OF BIOPHYSICS, 1976, 9 (02) :135-&
[4]   CRYSTAL-STRUCTURE OF THE COMPLEX OF RAT NEONATAL FC RECEPTOR WITH FC [J].
BURMEISTER, WP ;
HUBER, AH ;
BJORKMAN, PJ .
NATURE, 1994, 372 (6504) :379-383
[5]   THE BINDING-AFFINITY OF HUMAN-IGG FOR ITS HIGH-AFFINITY FC RECEPTOR IS DETERMINED BY MULTIPLE AMINO-ACIDS IN THE CH2 DOMAIN AND IS MODULATED BY THE HINGE REGION [J].
CANFIELD, SM ;
MORRISON, SL .
JOURNAL OF EXPERIMENTAL MEDICINE, 1991, 173 (06) :1483-1491
[6]   IDENTIFICATION OF THE FC-GAMMA RECEPTOR CLASS-I BINDING-SITE IN HUMAN-IGG THROUGH THE USE OF RECOMBINANT IGG1/IGG2 HYBRID AND POINT-MUTATED ANTIBODIES [J].
CHAPPEL, MS ;
ISENMAN, DE ;
EVERETT, M ;
XU, YY ;
DORRINGTON, KJ ;
KLEIN, MH .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (20) :9036-9040
[7]  
CHAPPEL MS, 1993, J BIOL CHEM, V268, P25124
[8]  
Coloma MJ, 1997, J IMMUNOL, V158, P733
[9]   CHANGES IN SPECIFIC SEQUESTRATION OF PROTEIN DURING TRANSPORT INTO DEVELOPING OOCYTE OF CHICKEN [J].
CUTTING, JA ;
ROTH, TF .
BIOCHIMICA ET BIOPHYSICA ACTA, 1973, 298 (04) :951-955