Literature DB >> 24641959

Cancer vaccine characterization: from bench to clinic.

K de la Luz-Hernández1, Y Rabasa2, R Montesinos3, D Fuentes4, J F Santo-Tomás2, O Morales2, Y Aguilar2, B Pacheco2, A Castillo2.   

Abstract

BACKGROUND: The development of safe, effective, and affordable vaccines has become a global effort due to its vast impact on overall world health conditions. A brief overview of vaccine characterization techniques, especially in the area of high-resolution mass spectrometry, is presented. It is highly conceivable that the proper use of advanced technologies such as high-resolution mass spectrometry, along with the appropriate chemical and physical property evaluations, will yield tremendous in-depth scientific understanding for the characterization of vaccines in various stages of vaccine development. This work presents the physicochemical and biological characterization of cancer vaccine Racotumomab/alumina, a murine anti-idiotypic antibody that mimics N-glycolyl-GM3 gangliosides. This antibody has been tested as an anti-idiotypic cancer vaccine, adjuvated in Al(OH)3, in several clinical trials for melanoma, breast, and lung cancer.
METHODS: Racotumomab was obtained from ascites fluid, transferred to fermentation in stirred tank at 10 L and followed to a scale up to 41 L. The mass spectrometry was used for the determination of intact molecule, light and heavy chains masses; amino acids sequence analysis, N- and C-terminal, glycosylation and posttranslational modifications. Also we used the DLS for the size distribution and zeta potential analysis. The biological analyses were performed in mice and chickens.
RESULTS: We observed differences in glycosylation pattern, charge heterogeneity and structural stability between in vivo-produced and bioreactor-obtained Racotumomab products. Interestingly, these modifications had no significant impact on the immune responses elicited in two different animal models.
CONCLUSIONS: We are demonstrated that this approach could potentially be more efficient and effective for supporting vaccine research and development.
Copyright © 2014. Published by Elsevier Ltd.

Entities:  

Keywords:  Cancer vaccine; Comparability studies; Mass spectrometry; Monoclonal antibody

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Year:  2014        PMID: 24641959     DOI: 10.1016/j.vaccine.2014.02.017

Source DB:  PubMed          Journal:  Vaccine        ISSN: 0264-410X            Impact factor:   3.641


  2 in total

1.  At least two Fc Neu5Gc residues of monoclonal antibodies are required for binding to anti-Neu5Gc antibody.

Authors:  Chuanfei Yu; Kai Gao; Lei Zhu; Wenbo Wang; Lan Wang; Feng Zhang; Chunyu Liu; Meng Li; Mark R Wormald; Pauline M Rudd; Junzhi Wang
Journal:  Sci Rep       Date:  2016-01-29       Impact factor: 4.379

Review 2.  From "Serum Sickness" to "Xenosialitis": Past, Present, and Future Significance of the Non-human Sialic Acid Neu5Gc.

Authors:  Chirag Dhar; Aniruddha Sasmal; Ajit Varki
Journal:  Front Immunol       Date:  2019-04-17       Impact factor: 7.561

  2 in total

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