Abstract
G7 and PNK-E mAbs recognize distinct porcine NK cell and granulocyte function-associated molecules that enhance and induce a significant cytolytic response against tumor cell targets through a mechanism of redirected cytotoxicity. The present study shows that the G7 and PNK-E molecules are present on the surface of porcine neutrophils, monocytes, and pulmonary alveolar macrophages as a physically and functionally associated cytolytic trigger molecular complex. Two-color flow cytometric analysis demonstrates that most, if not all, neutrophils are G7 and PNK-E antigen positive. In contrast, monocytes and PAM contain both G7 and PNK-E positive as well as G7 positive and PNK-E negative subpopulations. mAb binding competition experiments indicate that pretreatment of phagocytes with G7 mAb can block subsequent binding by PNK-E mAb, suggesting that these antigens are physically associated on the surface of porcine phagocytes. Fluorescent co-capping experiments utilizing G7 and PNK-E mAbs clearly demonstrate a physical association between G7 and PNK-E antigens present on the surface of porcine neutrophils. Pretreatment of phagocytes with F(ab’)2 fragments of G7 and PNK-E mAbs shows that F(ab’)2 G7 mAb blocks subsequent induction of phagocyte-mediated tumor cell cytotoxicity by whole PNK-E mAb but pretreatment with F(ab’)2 PNK-E does not block subsequent induction of phagocyte-mediated tumor cell cytotoxicity by whole G7 mAb. In addition, pretreatment of neutrophils and mononuclear phagocytes with F(ab’)2 fragments of G7 mAb blocks subsequent whole PNK-E mAb-dependent activation of a phagocytic cell intracellular oxidative burst response but pretreatment with F(ab’)2 PNK-E does not block subsequent G7 mAb-dependent activation of a phagocytic cell intracellular oxidative burst response. These data reinforce a physical and functional association between the G7 and PNK-E molecules. Recent identification of the G7 antigen as the porcine homolog of FcγRIII indicates that the G7 and PNK-E mAbs recognize a unique and previously uncharacterized FcγR cytolytic trigger molecular complex present on the surface of porcine neutrophils, monocytes, and PAM.
| Original language | English |
|---|---|
| Pages (from-to) | 270-278 |
| Number of pages | 9 |
| Journal | Cellular Immunology |
| Volume | 161 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1995 Jan 1 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Immunology
Cite this
Characterization of the cytolytic trigger molecules G7/PNK-E as a molecular complex on the surface of porcine phagocytes. / Aller, Steve C.; Cho, Dae Ho; Kim, Yoon B.
In: Cellular Immunology, Vol. 161, No. 2, 01.01.1995, p. 270-278.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterization of the cytolytic trigger molecules G7/PNK-E as a molecular complex on the surface of porcine phagocytes
AU - Aller, Steve C.
AU - Cho, Dae Ho
AU - Kim, Yoon B.
PY - 1995/1/1
Y1 - 1995/1/1
N2 - G7 and PNK-E mAbs recognize distinct porcine NK cell and granulocyte function-associated molecules that enhance and induce a significant cytolytic response against tumor cell targets through a mechanism of redirected cytotoxicity. The present study shows that the G7 and PNK-E molecules are present on the surface of porcine neutrophils, monocytes, and pulmonary alveolar macrophages as a physically and functionally associated cytolytic trigger molecular complex. Two-color flow cytometric analysis demonstrates that most, if not all, neutrophils are G7 and PNK-E antigen positive. In contrast, monocytes and PAM contain both G7 and PNK-E positive as well as G7 positive and PNK-E negative subpopulations. mAb binding competition experiments indicate that pretreatment of phagocytes with G7 mAb can block subsequent binding by PNK-E mAb, suggesting that these antigens are physically associated on the surface of porcine phagocytes. Fluorescent co-capping experiments utilizing G7 and PNK-E mAbs clearly demonstrate a physical association between G7 and PNK-E antigens present on the surface of porcine neutrophils. Pretreatment of phagocytes with F(ab’)2 fragments of G7 and PNK-E mAbs shows that F(ab’)2 G7 mAb blocks subsequent induction of phagocyte-mediated tumor cell cytotoxicity by whole PNK-E mAb but pretreatment with F(ab’)2 PNK-E does not block subsequent induction of phagocyte-mediated tumor cell cytotoxicity by whole G7 mAb. In addition, pretreatment of neutrophils and mononuclear phagocytes with F(ab’)2 fragments of G7 mAb blocks subsequent whole PNK-E mAb-dependent activation of a phagocytic cell intracellular oxidative burst response but pretreatment with F(ab’)2 PNK-E does not block subsequent G7 mAb-dependent activation of a phagocytic cell intracellular oxidative burst response. These data reinforce a physical and functional association between the G7 and PNK-E molecules. Recent identification of the G7 antigen as the porcine homolog of FcγRIII indicates that the G7 and PNK-E mAbs recognize a unique and previously uncharacterized FcγR cytolytic trigger molecular complex present on the surface of porcine neutrophils, monocytes, and PAM.
AB - G7 and PNK-E mAbs recognize distinct porcine NK cell and granulocyte function-associated molecules that enhance and induce a significant cytolytic response against tumor cell targets through a mechanism of redirected cytotoxicity. The present study shows that the G7 and PNK-E molecules are present on the surface of porcine neutrophils, monocytes, and pulmonary alveolar macrophages as a physically and functionally associated cytolytic trigger molecular complex. Two-color flow cytometric analysis demonstrates that most, if not all, neutrophils are G7 and PNK-E antigen positive. In contrast, monocytes and PAM contain both G7 and PNK-E positive as well as G7 positive and PNK-E negative subpopulations. mAb binding competition experiments indicate that pretreatment of phagocytes with G7 mAb can block subsequent binding by PNK-E mAb, suggesting that these antigens are physically associated on the surface of porcine phagocytes. Fluorescent co-capping experiments utilizing G7 and PNK-E mAbs clearly demonstrate a physical association between G7 and PNK-E antigens present on the surface of porcine neutrophils. Pretreatment of phagocytes with F(ab’)2 fragments of G7 and PNK-E mAbs shows that F(ab’)2 G7 mAb blocks subsequent induction of phagocyte-mediated tumor cell cytotoxicity by whole PNK-E mAb but pretreatment with F(ab’)2 PNK-E does not block subsequent induction of phagocyte-mediated tumor cell cytotoxicity by whole G7 mAb. In addition, pretreatment of neutrophils and mononuclear phagocytes with F(ab’)2 fragments of G7 mAb blocks subsequent whole PNK-E mAb-dependent activation of a phagocytic cell intracellular oxidative burst response but pretreatment with F(ab’)2 PNK-E does not block subsequent G7 mAb-dependent activation of a phagocytic cell intracellular oxidative burst response. These data reinforce a physical and functional association between the G7 and PNK-E molecules. Recent identification of the G7 antigen as the porcine homolog of FcγRIII indicates that the G7 and PNK-E mAbs recognize a unique and previously uncharacterized FcγR cytolytic trigger molecular complex present on the surface of porcine neutrophils, monocytes, and PAM.
UR - http://www.scopus.com/inward/record.url?scp=0028906834&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028906834&partnerID=8YFLogxK
U2 - 10.1006/cimm.1995.1036
DO - 10.1006/cimm.1995.1036
M3 - Article
C2 - 7697738
AN - SCOPUS:0028906834
VL - 161
SP - 270
EP - 278
JO - Cellular Immunology
JF - Cellular Immunology
SN - 0008-8749
IS - 2
ER -