PMID- 14580997
OWN - NLM
STAT- MEDLINE
DCOM- 20031202
LR  - 20190610
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1652
IP  - 1
DP  - 2003 Nov 3
TI  - Localization of ligand-binding sites on human C1q globular head region using 
      recombinant globular head fragments and single-chain antibodies.
PG  - 64-74
AB  - As a charge pattern recognition molecule, human C1q can bind a range of 
      immunoglobulin and non-immunoglobulin ligands via its carboxy-terminal globular 
      domain and activate the classical complement pathway. Each globular domain has a 
      heterotrimeric organization, composed of the carboxy-terminal halves of one A 
      (ghA), one B (ghB), and one C (ghC) chain. Recently, we have found that the 
      recombinant forms of individual ghA, ghB and ghC bind differentially to IgG, IgM, 
      gp41 peptide 601-613 of human immunodeficiency virus-1 (HIV-1), gp21 peptide 
      400-429 of human T cell lymphotrophic virus-I (HTLV-I), beta-amyloid peptide, and 
      apoptotic cells, suggesting a modular organization of the globular domain. This 
      paper examines the interaction of ghA, ghB and ghC with two known C1q ligands: 
      Klebsiella pneumoniae porin OmpK36 and salivary agglutinin. In addition, we have 
      used a panel of recombinant single-chain antibodies (scFv) specific for ghA, ghB 
      and ghC in order to map sites on the heterotrimeric globular domain which are 
      likely to interact with IgG1, IgG3, IgM, OmpK36, salivary agglutinin and gp41 
      loop peptide. The combined use of recombinant ghA, ghB, ghC and single-chain 
      antibodies has revealed at least three ligand-binding sites on the globular 
      domain of C1q: one is IgG- and OmpK36-specific, the second (IgM-binding site) is 
      most likely overlapping with IgG/OmpK36 binding site, and the third (the 
      gp41-binding site) seems to be located at the junction between the collagen and 
      globular domains.
FAU - Kojouharova, Mihaela S
AU  - Kojouharova MS
AD  - Department of Biochemistry, Sofia University, St. Kliment Ohridski, 8 Dragan 
      Tzankov Str, Sofia 1164, Bulgaria.
FAU - Tsacheva, Ivanka G
AU  - Tsacheva IG
FAU - Tchorbadjieva, Magdalena I
AU  - Tchorbadjieva MI
FAU - Reid, Kenneth B M
AU  - Reid KB
FAU - Kishore, Uday
AU  - Kishore U
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Agglutinins)
RN  - 0 (Bacterial Outer Membrane Proteins)
RN  - 0 (HIV Envelope Protein gp41)
RN  - 0 (Immunoglobulin Fragments)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Immunoglobulin M)
RN  - 0 (Ligands)
RN  - 0 (Peptide Fragments)
RN  - 0 (Porins)
RN  - 0 (Recombinant Proteins)
RN  - 80295-33-6 (Complement C1q)
SB  - IM
MH  - Agglutinins/metabolism
MH  - Antibody Specificity
MH  - Bacterial Outer Membrane Proteins/metabolism
MH  - Binding Sites
MH  - Complement C1q/*chemistry/genetics/immunology/*metabolism
MH  - HIV Envelope Protein gp41/immunology/metabolism
MH  - Humans
MH  - Immunoglobulin Fragments/genetics/immunology/*metabolism
MH  - Immunoglobulin G/immunology/metabolism
MH  - Immunoglobulin M/immunology/metabolism
MH  - Klebsiella pneumoniae/chemistry
MH  - Ligands
MH  - Peptide Fragments/genetics/*metabolism
MH  - Porins/metabolism
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Recombinant Proteins/genetics/immunology/metabolism
MH  - Salivary Glands/chemistry
EDAT- 2003/10/29 05:00
MHDA- 2003/12/03 05:00
CRDT- 2003/10/29 05:00
PHST- 2003/10/29 05:00 [pubmed]
PHST- 2003/12/03 05:00 [medline]
PHST- 2003/10/29 05:00 [entrez]
AID - S157096390300270X [pii]
AID - 10.1016/j.bbapap.2003.08.003 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2003 Nov 3;1652(1):64-74. doi: 
      10.1016/j.bbapap.2003.08.003.