Quantification in Enzyme-Linked Immunosorbent Assay of a C3 Neoepitope Expressed on Activated Human Complement Factor C3

1988 ◽  
Vol 27 (3) ◽  
pp. 329-335 ◽  
Author(s):  
P. GARRED ◽  
T. E. MOLLNES ◽  
T. LEA
Keyword(s):  
Immunosorbent Assay ◽  
Enzyme Linked Immunosorbent Assay ◽  
Complement Factor ◽  
Human Complement ◽  
Complement Factor C3

scholarly journals Amino acid sequence of the trypsin-generated C3d fragment from human complement factor C3

1985 ◽  
Vol 230 (2) ◽  
pp. 353-361 ◽  
Author(s):  
U Hellman ◽  
G Eggertsen ◽  
A Engström ◽  
J Sjöquist
Keyword(s):  
Staphylococcus Aureus ◽  
Cdna Sequence ◽  
Sequence Data ◽  
Reversed Phase ◽  
Complement Factor ◽  
Edman Degradation ◽  
Human Complement ◽  
Complete Sequences ◽  
Cnbr Cleavage ◽  
Complement Factor C3

Human C3d (try-C3d), prepared from trypsin-digested C3, was fragmented by cleavage with CNBr. Eight peptides were defined and separated by h.p.l.c. on reversed-phase columns. By automatic Edman degradation the complete sequences of five peptides and partial sequences of three peptides were determined. To obtain overlapping peptides the latter three fragments were digested with trypsin, chymotrypsin or Staphylococcus aureus V8 proteinase, after which the fragments were separated on reversed-phase columns. Two of the CNBr-cleavage peptides were completely sequenced, and 70% of the sequence of the remaining CNBr-cleavage peptide was determined. The non-sequenced part represents a very hydrophobic segment of try-C3d. The sequence data obtained represent 90% of the primary structure of try-C3d. Alignment of the CNBr-cleavage fragments was made easier by comparison with the cDNA sequence of mouse pro-C3 [Wetsel, Lundwall, Davidson, Gibson, Tack & Fey (1984) J. Biol. Chem. 259, 13857-13862]. Comparison of try-C3d with the equivalent part of human C4B revealed an extensive sequence homology in the N-terminal half of the molecules.

scholarly journals Chemical characterization of cyanogen bromide fragments from the β-chain of human complement factor C3

FEBS Letters ◽  
1984 ◽  
Vol 169 (1) ◽  
pp. 57-62 ◽  
Author(s):  
Åke Lundwall ◽  
Ulf Hellman ◽  
Gösta Eggertsen ◽  
John Sjöquist
Keyword(s):  
Cyanogen Bromide ◽  
Chemical Characterization ◽  
Complement Factor ◽  
Human Complement ◽  
Complement Factor C3 ◽  
Β Chain

Characterization of tryptic fragments of human complement factor C3

1985 ◽  
Vol 22 (8) ◽  
pp. 833-841 ◽  
Author(s):  
Gösta Eggertsen ◽  
Ulf Hellman ◽  
Åake Lundwall ◽  
Jørgen Folkersen ◽  
John Sjöquist
Keyword(s):  
Complement Factor ◽  
Human Complement ◽  
Complement Factor C3

scholarly journals Complement activation in individuals with previous subclinical Lyme borreliosis and patients with previous Lyme neuroborreliosis

2019 ◽  
Vol 39 (5) ◽  
pp. 855-862
Author(s):  
Hanna Carlsson ◽  
Kerstin Sandholm ◽  
Haben Woldu Haddish ◽  
Lars Brudin ◽  
Kristina Nilsson Ekdahl ◽  
...  
Keyword(s):  
Lyme Borreliosis ◽  
Complement Activation ◽  
Clinical Manifestations ◽  
Lyme Neuroborreliosis ◽  
Enzyme Linked Immunosorbent Assay ◽  
Complement Factor ◽  
Significant Difference ◽  
Activation Products ◽  
Study Population ◽  
Complement Factor C3

AbstractLyme borreliosis (LB) is caused by Borrelia burgdorferi and infection may lead to not only a large variety of clinical manifestations but also a subclinical outcome. The aim of the present study was to investigate if there is a constitutional difference in complement activation between individuals with previous subclinical Lyme borreliosis (SB) and patients previously diagnosed with Lyme neuroborreliosis (LNB).Lepirudin plasma for activation studies was collected from 60 SB individuals and from 22 patients pre-diagnosed with LNB. The plasma was incubated with live Borrelia spirochetes of two strains (complement sensitive B. garinii Lu59 and complement resistant B. afzelii ACA1).Complement factor C3 was measured in non-activated lepirudin plasma with immune-nephelometry and C3a and sC5b-9 generated during complement activation were measured by enzyme-linked immunosorbent assay.We found that the complement sensitive Lu59 induced higher complement activation than the complement resistant ACA1 when measuring activation products C3a and sC5b-9 in SB and LNB patients, p < 0.0001. No significant difference was found between SB and LNB patients in systemic levels of C3. Furthermore, SB individuals generated a higher activation of C3 cleavage to C3a (C3a/C3 ratio) than LNB patients after activation with ACA1, p < 0.001, but no significant differences were found in response to Lu59. In conclusion, Lu59 induced higher complement activation than ACA1 and individuals with previous SB showed increased generation of C3a compared with patients with previous LNB. In our study population, this mechanism could lead to less elimination of spirochetes in LNB patients and thereby be a factor contributing to the clinical outcome.

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