Publications by authors named "M Occhino"

Article Synopsis
  • Recombinant-tagged proteins are valuable in research and clinical applications, but creating different tagged versions of the same protein can be complicated and time-consuming due to complex cloning processes.
  • This study introduces a novel vector system that streamlines the production of various tagged protein variants using a single DNA fragment and multiple ready-to-use vectors, each equipped with a different tag.
  • The expression system is validated by successfully producing a functional anti-GD2 Fab fragment that can be tagged with biotin, polyhistidine, or both, demonstrating that the protein functions effectively with these tags.
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UL18 is a trans-membrane viral protein expressed on human cytomegalovirus (HCMV)-infected cells, and its surface expression determines the interaction of infected cells with lymphocytes expressing the CD85j (LIR-1/ILT2) receptor. We previously showed that the UL18-CD85j interaction elicits activation of T lymphocytes. However, in in vitro cell models UL18 displays mostly undetectable surface expression.

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UL18 is a glycoprotein encoded by the human cytomegalovirus genome and is thought to play a pivotal role during human cytomegalovirus infection, although its exact function is still a matter of debate. UL18 shares structural similarity with MHC class I and binds the receptor CD85j on immune cells. Besides UL18, CD85j binds MHC class I molecules.

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Purpose: Detection of metastatic tumor cells in bone marrow (BM) and peripheral blood (PB) of children with neuroblastoma is crucial for prognosis and planning of therapy. Aims of this large descriptive repeated survey were to evaluate the diagnostic accuracy of different techniques in diagnostic samples obtained at several disease course time points and to correlate positive results with patient clinical features and outcome.

Experimental Design: BM aspirates, trephine biopsies, PB, and peripheral blood stem cell (PBSC) samples from Italian children with neuroblastoma were analyzed by morphological and histologic techniques, as well as by immunocytochemistry (IC) for disialoganglioside GD(2) and reverse transcription-PCRs (RT-PCRs) for tyrosine hydroxylase (TH) and pgp9.

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GD2 is a disialoganglioside expressed at high density on the surface of malignant cells of neuroectodermal origin, especially in neuroblastoma (NB) and melanoma. Since its expression in normal tissues is very restricted, GD2 represents an excellent target for neuroectodermal tumor targeting. Mini-antibody technology allows the production of dimeric single-chain antibodies, also called small immunoproteins (SIPs), which are composed of a scFv fused to a dimerizing domain of immunoglobulin heavy chains.

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