Amino acid sequence of a CNBr fragment of human complement component Cls containing the active-site serine residue

1982 ◽  
Vol 10 (6) ◽  
pp. 441-442 ◽  
Author(s):  
PHILIP E. CARTER ◽  
BRYAN DUNBAR ◽  
JOHN E. FOTHERGILL
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Site ◽  
Complement Component ◽  
Human Complement ◽  
Serine Residue ◽  
Human Complement Component

scholarly journals Nucleotide sequence of cDNA and derived amino acid sequence of human complement component C9.

1984 ◽  
Vol 81 (23) ◽  
pp. 7298-7302 ◽  
Author(s):  
R. G. DiScipio ◽  
M. R. Gehring ◽  
E. R. Podack ◽  
C. C. Kan ◽  
T. E. Hugli ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Complement Component ◽  
Human Complement ◽  
Human Complement Component

scholarly journals Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence

1987 ◽  
Vol 169 (3) ◽  
pp. 547-553 ◽  
Author(s):  
Charlotte M. MACKINNON ◽  
Philip E. CARTER ◽  
S. Jane SMYTH ◽  
Bryan DUNBAR ◽  
John E. FOTHERGILL
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Cloning ◽  
Complement Component ◽  
Human Complement ◽  
Complete Amino Acid Sequence ◽  
Human Complement Component

scholarly journals Mycobacterial Protein HbhA Binds Human Complement Component C3

2001 ◽  
Vol 69 (12) ◽  
pp. 7501-7511 ◽  
Author(s):  
Stacey L. Mueller-Ortiz ◽  
Audrey R. Wanger ◽  
Steven J. Norris
Keyword(s):  
Amino Acid ◽  
Cell Membrane ◽  
Binding Protein ◽  
Complement Component ◽  
Mononuclear Phagocytes ◽  
Full Length ◽  
Dependent Manner ◽  
Human Complement ◽  
Complement Component C3 ◽  
Human Complement Component

ABSTRACT Mycobacterium tuberculosis and Mycobacterium avium are facultative intracellular pathogens that are able to survive and replicate in mononuclear phagocytes. Human complement component C3 has previously been shown to mediate attachment and phagocytosis of these bacteria by mononuclear phagocytes. In this study, a C3 ligand affinity blot protocol was used to identify a 30-kDa C3-binding protein in M. tuberculosis andMycobacterium smegmatis and a 31-kDa C3-binding protein inM. avium. The C3-binding proteins in M. tuberculosis and M. avium localized to the cell membrane fraction and partitioned to the detergent fraction during Triton X-114 phase partitioning. The C3-binding protein from M. tuberculosis was partially purified using a cation exchange column and was shown to bind concanavalin A. The N terminus and an internal fragment of the partially purified C3-binding protein were subjected to amino acid sequence analysis. The resulting amino acid sequences matched the M. tuberculosis heparin-binding hemagglutinin (HbhA) protein. Recombinant full-length HbhA and the C terminus of HbhA fused to maltose-binding protein, but not recombinant HbhA lacking the C-terminal region, bound human C3. Recombinant full-length HbhA coated on polystyrene beads, was found to enhance the adherence and/or phagocytosis of the coated beads to J774.A1 cells in both the presence and absence of human serum. The presence of complement-sufficient serum increased the adherence of the HbhA-coated beads to the J774.A1 cells in a C3-dependent manner. If HbhA within the bacterial cell membrane functions similarly to isolated HbhA, this protein may enhance the adherence and phagocytosis of M. tuberculosis and M. avium to mononuclear phagocytes through the binding of C3 and interaction with C3 receptors on mononuclear phagocytes.

scholarly journals The reactive serine residue of epidermolytic toxin A

1990 ◽  
Vol 269 (2) ◽  
pp. 535-537 ◽  
Author(s):  
C J Bailey ◽  
T P Smith
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Site ◽  
Functional Relationship ◽  
Sequence Data ◽  
Serine Residue ◽  
Toxin A ◽  
Amino Acid Sequence Data

Comparison of amino acid sequence data suggested that there may be a functional relationship between the staphylococcal epidermolytic toxins and V8 proteinase. The hypothesis was tested by treating epidermolytic toxin with di-isopropyl phosphorofluoridate, which bound specifically at serine-195, the homologue of the active-site serine residue of V8 proteinase.

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