Structure and Evolutionary Origin of the Gene Encoding a Human Serum Mannose-Binding Protein

1989 ◽  
Vol 77 (s21) ◽  
pp. 2P-2P
Author(s):  
John A. Summerfield ◽  
Maureen E. Taylor ◽  
Paul M. Brickell ◽  
Roger K. Craig
1989 ◽  
Vol 9 ◽  
pp. S88
Author(s):  
John A. Summerfield ◽  
Maureen E. Taylor ◽  
Paul M. Brickell ◽  
Roger K. Craig

1989 ◽  
Vol 262 (3) ◽  
pp. 763-771 ◽  
Author(s):  
M E Taylor ◽  
P M Brickell ◽  
R K Craig ◽  
J A Summerfield

The N-terminal sequence of the major human serum mannose-binding protein (MBP1) was shown to be identical at all positions determined with the amino acid sequence predicted from a cDNA clone of a human liver MBP mRNA. An oligonucleotide corresponding to part of the sequence of this cDNA clone was used to isolate a cosmid genomic clone containing a homologous gene. The intron/exon structure of this gene was found to closely resemble that of the gene encoding a rat liver MBP (MBP A). The nucleotide sequence of the exons differed in several places from that of the human cDNA clone published by Ezekowitz, Day & Herman [(1988) J. Exp. Med. 167, 1034-1046]. The MBP molecule comprises a signal peptide, a cysteine-rich domain, a collagen-like domain, a ‘neck’ region and a carbohydrate-binding domain. Each domain is encoded by a separate exon. This genomic organization lends support to the hypothesis that the gene arose during evolution by a process of exon shuffling. Several consensus sequences that may be involved in controlling the expression of human serum MBP have been identified in the promoter region of the gene. The consensus sequences are consistent with the suggestion that this mammalian serum lectin is regulated as an acute-phase protein synthesized by the liver.


1989 ◽  
Vol 169 (1) ◽  
pp. 185-196 ◽  
Author(s):  
R A Ezekowitz ◽  
M Kuhlman ◽  
J E Groopman ◽  
R A Byrn

In vitro infection by the human immunodeficiency virus (HIV) of CD4+ H9 lymphoblasts is inhibited by a mannose-binding protein (MBP) purified from human serum. In addition, MBP is able to selectively bind to HIV-infected H9 cells and HIV-infected cells from the monocyte cell line U937. These results indicate MBP most likely recognizes high mannose glycans known to be present on gp120 in the domain that is recognized by CD4 and thereby inhibits viral entry to susceptible cells. In support of this contention, recombinant gp120 binds directly to MBP; the binding is saturable, mannan inhibitable, removed by N-glycanase treatment, and dependent on divalent cations.


Biochemistry ◽  
1985 ◽  
Vol 24 (21) ◽  
pp. 5932-5938 ◽  
Author(s):  
Ke Yi Wang ◽  
Theresa B. Kuhlenschmidt ◽  
Y. C. Lee

Biochemistry ◽  
1999 ◽  
Vol 38 (22) ◽  
pp. 7321-7331 ◽  
Author(s):  
Hirofumi Chiba ◽  
Hitomi Sano ◽  
Masaki Saitoh ◽  
Hitoshi Sohma ◽  
Dennis R. Voelker ◽  
...  

2019 ◽  
Vol 519 (4) ◽  
pp. 773-776 ◽  
Author(s):  
Najwa Nabila ◽  
Vincencius F. Meidianto ◽  
Raymond R. Tjandrawinata ◽  
Heni Rachmawati ◽  
Wangsa T. Ismaya

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