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A human, compact, fully functional anti-ErbB2 antibody as a novel antitumour agent.

De Lorenzo C, Tedesco A, Terrazzano G, Cozzolino R, Laccetti P, Piccoli R, D'Alessio G - Br. J. Cancer (2004)

Bottom Line: A new human, compact antibody was engineered by fusion of a human, antitumour ErbB2-directed scFv with a human IgG1 Fc domain.This new immunoagent meets all criteria for a potential anticancer drug: it is human, hence poorly or not immunogenic; it binds selectively and with high affinity to target cells, on which it exerts an effective and selective antiproliferative action, including both antibody-dependent and complement-dependent cytotoxicity; it effectively inhibits tumour growth in vivo.Its compact molecular size should provide for an efficient tissue penetration, yet suitable to a prolonged serum half-life.

View Article: PubMed Central - PubMed

Affiliation: Department of Biological Chemistry, University of Naples Federico II, Via Mezzocannone 16, 80134 Naples, Italy.

ABSTRACT
A new human, compact antibody was engineered by fusion of a human, antitumour ErbB2-directed scFv with a human IgG1 Fc domain. Overexpression of the ErbB2 receptor is related to tumour aggressiveness and poor prognosis. This new immunoagent meets all criteria for a potential anticancer drug: it is human, hence poorly or not immunogenic; it binds selectively and with high affinity to target cells, on which it exerts an effective and selective antiproliferative action, including both antibody-dependent and complement-dependent cytotoxicity; it effectively inhibits tumour growth in vivo. Its compact molecular size should provide for an efficient tissue penetration, yet suitable to a prolonged serum half-life.

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Related in: MedlinePlus

Effects of Erb-hcAb on ErbB2-positive (SKBR3) and ErbB2-negative (A431) cells. (A) ELISA assays of SKBR3 cells (black symbols) and A431 cells (empty symbols) tested with Erb-hcAb (circles), the parental anti-ErbB2 scFv (rhomboids), or Herceptin (squares). (B) Dose–response curves for ErbB2-positive SKBR3 cells (black symbols), or ErbB2-negative A431 cells (empty symbols), treated for 72 h with Erb-hcAb (circles), or Herceptin (squares).
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fig2: Effects of Erb-hcAb on ErbB2-positive (SKBR3) and ErbB2-negative (A431) cells. (A) ELISA assays of SKBR3 cells (black symbols) and A431 cells (empty symbols) tested with Erb-hcAb (circles), the parental anti-ErbB2 scFv (rhomboids), or Herceptin (squares). (B) Dose–response curves for ErbB2-positive SKBR3 cells (black symbols), or ErbB2-negative A431 cells (empty symbols), treated for 72 h with Erb-hcAb (circles), or Herceptin (squares).

Mentions: When the ability of the recombinant fusion protein to bind ErbB2-positive cells was analysed by ELISA assays (Figure 2AFigure 2


A human, compact, fully functional anti-ErbB2 antibody as a novel antitumour agent.

De Lorenzo C, Tedesco A, Terrazzano G, Cozzolino R, Laccetti P, Piccoli R, D'Alessio G - Br. J. Cancer (2004)

Effects of Erb-hcAb on ErbB2-positive (SKBR3) and ErbB2-negative (A431) cells. (A) ELISA assays of SKBR3 cells (black symbols) and A431 cells (empty symbols) tested with Erb-hcAb (circles), the parental anti-ErbB2 scFv (rhomboids), or Herceptin (squares). (B) Dose–response curves for ErbB2-positive SKBR3 cells (black symbols), or ErbB2-negative A431 cells (empty symbols), treated for 72 h with Erb-hcAb (circles), or Herceptin (squares).
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2747711&req=5

fig2: Effects of Erb-hcAb on ErbB2-positive (SKBR3) and ErbB2-negative (A431) cells. (A) ELISA assays of SKBR3 cells (black symbols) and A431 cells (empty symbols) tested with Erb-hcAb (circles), the parental anti-ErbB2 scFv (rhomboids), or Herceptin (squares). (B) Dose–response curves for ErbB2-positive SKBR3 cells (black symbols), or ErbB2-negative A431 cells (empty symbols), treated for 72 h with Erb-hcAb (circles), or Herceptin (squares).
Mentions: When the ability of the recombinant fusion protein to bind ErbB2-positive cells was analysed by ELISA assays (Figure 2AFigure 2

Bottom Line: A new human, compact antibody was engineered by fusion of a human, antitumour ErbB2-directed scFv with a human IgG1 Fc domain.This new immunoagent meets all criteria for a potential anticancer drug: it is human, hence poorly or not immunogenic; it binds selectively and with high affinity to target cells, on which it exerts an effective and selective antiproliferative action, including both antibody-dependent and complement-dependent cytotoxicity; it effectively inhibits tumour growth in vivo.Its compact molecular size should provide for an efficient tissue penetration, yet suitable to a prolonged serum half-life.

View Article: PubMed Central - PubMed

Affiliation: Department of Biological Chemistry, University of Naples Federico II, Via Mezzocannone 16, 80134 Naples, Italy.

ABSTRACT
A new human, compact antibody was engineered by fusion of a human, antitumour ErbB2-directed scFv with a human IgG1 Fc domain. Overexpression of the ErbB2 receptor is related to tumour aggressiveness and poor prognosis. This new immunoagent meets all criteria for a potential anticancer drug: it is human, hence poorly or not immunogenic; it binds selectively and with high affinity to target cells, on which it exerts an effective and selective antiproliferative action, including both antibody-dependent and complement-dependent cytotoxicity; it effectively inhibits tumour growth in vivo. Its compact molecular size should provide for an efficient tissue penetration, yet suitable to a prolonged serum half-life.

Show MeSH
Related in: MedlinePlus