THE FUNCTIONAL UNITS OF A PEPTOSTREPTOCOCCAL PROTEIN-L

被引:26
作者
MURPHY, JP [1 ]
DUGGLEBY, CJ [1 ]
ATKINSON, MA [1 ]
TROWERN, AR [1 ]
ATKINSON, T [1 ]
GOWARD, CR [1 ]
机构
[1] PUBL HLTH LAB SERV,CTR APPL MICROBIOL & RES,DIV BIOTECHNOL,SALISBURY SP4 0JQ,WILTS,ENGLAND
关键词
D O I
10.1111/j.1365-2958.1994.tb01079.x
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
Protein L is a cell-surface protein from Peptostreptococcus which interacts with immunoglobulin kappa light chains. A gene from Peptostreptococcus strain 3316 coding for protein L and fragments thereof were expressed in Escherichia coli. The peptides were examined for binding to immunoglobulin and serum albumin. The four C units were shown to be responsible for binding to immunoglobulin and the four D units for binding to albumin. This protein L molecule therefore binds to albumin at a site separate from that involved in binding to immunoglobulin. The albumin-binding units have high amino acid sequence identity with the albumin-binding units of streptococcal cell-surface proteins. The gene contains three sites available for Internal initiation of translation resulting in three active proteins. The protein L molecule presented in this report was compared with a previously reported protein from Peptostreptococcus strain 312. The two proteins differ in several respects, including size and the number and types of repeat units.
引用
收藏
页码:911 / 920
页数:10
相关论文
共 38 条
[1]  
BJORCK L, 1988, J IMMUNOL, V140, P1194
[2]   STREPTOCOCCAL PROTEIN-G, EXPRESSED BY STREPTOCOCCI OR BY ESCHERICHIA-COLI, HAS SEPARATE BINDING-SITES FOR HUMAN-ALBUMIN AND IGG [J].
BJORCK, L ;
KASTERN, W ;
LINDAHL, G ;
WIDEBACK, K .
MOLECULAR IMMUNOLOGY, 1987, 24 (10) :1113-1122
[3]  
BREHM JK, 1991, APPL MICROBIOL BIOT, V36, P358
[4]   THE PMTL NIC-CLONING VECTORS .1. IMPROVED PUC POLYLINKER REGIONS TO FACILITATE THE USE OF SONICATED DNA FOR NUCLEOTIDE SEQUENCING [J].
CHAMBERS, SP ;
PRIOR, SE ;
BARSTOW, DA ;
MINTON, NP .
GENE, 1988, 68 (01) :139-149
[5]   NONCHROMOSOMAL ANTIBIOTIC RESISTANCE IN BACTERIA - GENETIC TRANSFORMATION OF ESCHERICHIA-COLI BY R-FACTOR DNA [J].
COHEN, SN ;
CHANG, ACY ;
HSU, L .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1972, 69 (08) :2110-&
[6]  
DECHATEAU M, 1993, SCAND J IMMUNOL, V37, P399
[7]   CRYSTAL-STRUCTURE OF A STREPTOCOCCAL PROTEIN-G DOMAIN BOUND TO AN FAB FRAGMENT [J].
DERRICK, JP ;
WIGLEY, DB .
NATURE, 1992, 359 (6397) :752-754
[8]   A COMPREHENSIVE SET OF SEQUENCE-ANALYSIS PROGRAMS FOR THE VAX [J].
DEVEREUX, J ;
HAEBERLI, P ;
SMITHIES, O .
NUCLEIC ACIDS RESEARCH, 1984, 12 (01) :387-395
[9]   PROGRESSIVE SEQUENCE ALIGNMENT AS A PREREQUISITE TO CORRECT PHYLOGENETIC TREES [J].
FENG, DF ;
DOOLITTLE, RF .
JOURNAL OF MOLECULAR EVOLUTION, 1987, 25 (04) :351-360
[10]   CONVERGENT EVOLUTION AMONG IMMUNOGLOBULIN-G-BINDING BACTERIAL PROTEINS [J].
FRICK, IM ;
WIKSTROM, M ;
FORSEN, S ;
DRAKENBERG, T ;
GOMI, H ;
SJOBRING, U ;
BJORCK, L .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (18) :8532-8536