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Recombinant Proteins 3.0
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Recombinant Proteins 3.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: closed (31 October 2022) | Viewed by 3801

Special Issue Editors

Prof. Dr. Karen A. McDonald

E-Mail Website
Guest Editor
Department of Chemical Engineering, University of California, Davis, CA 95616, USA
Interests: plant-based recombinant protein production; bioprocess engineering; techno-economic analyses
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Somen Nandi

E-Mail Website1 Website2
Guest Editor
Department of Chemical Engineering and Global HealthShare® Initiative, University of California, Davis, CA 95616, USA
Interests: recombinant protein expression; drug development; glycan modification; protein process engineering; process economics
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Issue is a continuation of our previous Special Issue “Recombinant Proteins” .

By simple definition, a recombinant protein is a protein encoded by a heterologous or synthetic gene(s)—recombinant DNA—that has been cloned in a system that supports expression of the gene(s) to produce messenger RNA (mRNA) followed by translation to protein and possibly post-translational modification and subcellular targeting. Modification of the gene by recombinant DNA technology can lead to expression of many proteins. Potential applications of these recombinant protein products include human and animal therapeutics, subunit vaccines, diagnostics, industrial enzymes, food additives or processing agents, crop protectant biologics, biopolymers, and reagents, to name a few. Although there are a variety of potential hosts and manufacturing strategies that are currently available or are being developed, each application has different constraints in terms of capital and manufacturing cost, production scale needed, quality and purity attributes, and regulatory requirements.

The focus of this Special Issue of the International Journal of Molecular Sciences (IJMS), entitled Recombinant Proteins, is the science and engineering of recombinant protein production, particularly production of complex and hard to produce proteins (membrane proteins, ones with solubility issues or requiring extensive post-translational modifications), transient production of recombinant proteins in a variety of hosts for rapid response, novel expression systems, host engineering and stability, secretion, localization and post-translational modifications, protein engineering including enzyme engineering, fusion proteins and biobetter biologics.

Prof. Dr. Karen A. McDonald
Prof. Dr. Somen Nandi
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Recombinant Proteins
  • Recombinant DNA
  • Rapid (e.g., transient) production
  • Scale-up of production platforms
  • New hosts for rapid production
  • Novel technologies to treat or prevent pathogens

Published Papers (2 papers)

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Research

13 pages, 4697 KiB  
Article
Regulatory T Cell Depletion Using a CRISPR Fc-Optimized CD25 Antibody
by Marit J. van Elsas, Johan M. S. van der Schoot, Alexander Bartels, Kas Steuten, Duco van Dalen, Zacharias Wijfjes, Carl G. Figdor, Thorbald van Hall, Sjoerd H. van der Burg, Martijn Verdoes and Ferenc A. Scheeren
Int. J. Mol. Sci. 2022, 23(15), 8707; https://doi.org/10.3390/ijms23158707 - 05 Aug 2022
Cited by 4 | Viewed by 2104
Abstract
Regulatory T cells (Tregs) are major drivers behind immunosuppressive mechanisms and present a major hurdle for cancer therapy. Tregs are characterized by a high expression of CD25, which is a potentially valuable target for Treg depletion to alleviate immune [...] Read more.
Regulatory T cells (Tregs) are major drivers behind immunosuppressive mechanisms and present a major hurdle for cancer therapy. Tregs are characterized by a high expression of CD25, which is a potentially valuable target for Treg depletion to alleviate immune suppression. The preclinical anti-CD25 (αCD25) antibody, clone PC-61, has met with modest anti-tumor activity due to its capacity to clear Tregs from the circulation and lymph nodes, but not those that reside in the tumor. The optimization of the Fc domain of this antibody clone has been shown to enhance the intratumoral Treg depletion capacity. Here, we generated a stable cell line that produced optimized recombinant Treg-depleting antibodies. A genome engineering strategy in which CRISPR-Cas9 was combined with homology-directed repair (CRISPR-HDR) was utilized to optimize the Fc domain of the hybridoma PC-61 for effector functions by switching it from its original rat IgG1 to a mouse IgG2a isotype. In a syngeneic tumor mouse model, the resulting αCD25-m2a (mouse IgG2a isotype) antibody mediated the effective depletion of tumor-resident Tregs, leading to a high effector T cell (Teff) to Treg ratio. Moreover, a combination of αCD25-m2a and an αPD-L1 treatment augmented tumor eradication in mice, demonstrating the potential for αCD25 as a cancer immunotherapy. Full article
(This article belongs to the Special Issue Recombinant Proteins 3.0)
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17 pages, 2357 KiB  
Article
Analysis of Variability of Functionals of Recombinant Protein Production Trajectories Based on Limited Data
by Shuting Liao, Kantharakorn Macharoen, Karen A. McDonald, Somen Nandi and Debashis Paul
Int. J. Mol. Sci. 2022, 23(14), 7628; https://doi.org/10.3390/ijms23147628 - 10 Jul 2022
Viewed by 1099
Abstract
Making statistical inference on quantities defining various characteristics of a temporally measured biochemical process and analyzing its variability across different experimental conditions is a core challenge in various branches of science. This problem is particularly difficult when the amount of data that can [...] Read more.
Making statistical inference on quantities defining various characteristics of a temporally measured biochemical process and analyzing its variability across different experimental conditions is a core challenge in various branches of science. This problem is particularly difficult when the amount of data that can be collected is limited in terms of both the number of replicates and the number of time points per process trajectory. We propose a method for analyzing the variability of smooth functionals of the growth or production trajectories associated with such processes across different experimental conditions. Our modeling approach is based on a spline representation of the mean trajectories. We also develop a bootstrap-based inference procedure for the parameters while accounting for possible multiple comparisons. This methodology is applied to study two types of quantities—the “time to harvest” and “maximal productivity”—in the context of an experiment on the production of recombinant proteins. We complement the findings with extensive numerical experiments comparing the effectiveness of different types of bootstrap procedures for various tests of hypotheses. These numerical experiments convincingly demonstrate that the proposed method yields reliable inference on complex characteristics of the processes even in a data-limited environment where more traditional methods for statistical inference are typically not reliable. Full article
(This article belongs to the Special Issue Recombinant Proteins 3.0)
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