Cristin-resultat-ID: 350560
Sist endret: 25. oktober 2016 14:35
Resultat
Vitenskapelig artikkel
1994

Human IgG isotype specific amino acid residues affecting complement mediated cel lysis and phagocytosis

Bidragsytere:
  • OH Brekke
  • Terje Einar Michaelsen
  • Audun Aase
  • Randi Helene Sandin og
  • I Sandlie

Tidsskrift

European Journal of Immunology
ISSN 0014-2980
e-ISSN 1521-4141
NVI-nivå 2

Om resultatet

Vitenskapelig artikkel
Publiseringsår: 1994
Volum: 24
Sider: 2542 - 2547

Beskrivelse Beskrivelse

Tittel

Human IgG isotype specific amino acid residues affecting complement mediated cel lysis and phagocytosis

Sammendrag

In this report we describe the construction of anti-5-iodo-4-hydroxy-3-nitrophenacetyl (NIP) mouse/human immunoglobulin (Ig) G4 chimeric molecules with altered amino acid residues in the CH2 domain. Three mutants are described. Gln-268 is substituted by His in gamma 4 Q268H, Ser-331 is substituted by Pro in gamma 4 S331P, and in gamma 4 Q268H/S331P both residues are substituted. The ability of the mutant molecules to induce complement-mediated cell lysis (CML) and phagocytosis by Fc gamma RII- and Fc gamma RIII-bearing polymorphonuclear leukocytes (PMN) were measured. In CML, gamma 4 Q268H was inactive, but both gamma 4 S331P and gamma 4 Q268H/S331P were active provided that the antigenic density on the target cells was high. In phagocytosis mediated by PMN, the mutants gamma 4 S331P and gamma 4 Q268H/S331P were both active only when complement was introduced. gamma 4 Q268H was not active in phagocytosis under any conditions. We conclude that His-268 in human IgG molecules does not modulate CML activity or phagocytosis mediated by Fc gamma RII and/or Fc gamma RIII. Pro-331 rescues CML activity in IgG4 molecules when the epitope density on the target cells is high, but does not affect Fc gamma RII/Fc gamma RIII-mediated phagocytosis. In this manner the mutants gamma 4 S331P and gamma 4 Q268H/S331P mimic human IgG2. This could indicate a structural similarity between IgG2 and these mutant molecules that distinguish them from both IgG1 and IgG3

Bidragsytere

Ole Henrik Brekke

Bidragsyterens navn vises på dette resultatet som OH Brekke
  • Tilknyttet:
    Forfatter

Terje Einar Michaelsen

  • Tilknyttet:
    Forfatter
    ved Folkehelseinstituttet
  • Tilknyttet:
    Forfatter
    ved Seksjon for farmasøytisk kjemi ved Universitetet i Oslo

Audun Aase

  • Tilknyttet:
    Forfatter
    ved Avdeling for infeksjonsimmunologi ved Folkehelseinstituttet

Randi Helene Sandin

  • Tilknyttet:
    Forfatter
    ved Folkehelseinstituttet

Inger Sandlie

Bidragsyterens navn vises på dette resultatet som I Sandlie
  • Tilknyttet:
    Forfatter
    ved Institutt for biovitenskap (tidl. IMBV) ved Universitetet i Oslo
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