Kemp Proteins LLC, a contract research and manufacturing organisation, announced on Thursday that it is expanding its cell line development and recombinant protein production capabilities through a strategic partnership with biotechnology company NeuImmune and its proprietary glycoengineered CHO (geCHO) BioDesign platform, bringing greater control over protein glycosylation to Kemp's gene-to-protein development workflow.

Glycosylation, the attachment of sugar structures to proteins, is a critical post-translational modification that can significantly influence protein efficacy, activity, stability, formulation, half-life, safety, immunogenicity, and other characteristics important to biologic development. Yet conventional recombinant protein expression frequently produces heterogeneous glycoforms that are largely determined by the production cell, making it difficult to systematically evaluate how alternative glycosylation patterns affect protein performance.

NeuImmune's geCHO BioDesign platform was developed to address this challenge by combining a panel of 28 geCHO cell lines built from a GMP-ready CHO-S parental cell line. The cells have been genome-edited and phenotype-confirmed to provide a broad range of N-glycan structures, including high-mannose, mono-, bi-, tri-, and tetra-antennary, fucosylated, afucosylated, as well as different sialylation profiles. Resulting protein variants can then be evaluated for attributes such as activity, stability, and half-life to help identify glycoforms associated with the required function and performance.

The platform also incorporates GlyCompare, part of NeuImmune's explanatory AI and systems-biology framework, which decomposes glycoprofiles into shared glycan substructures and uses those features to help identify the glycan characteristics associated with specific phenotypic responses. This approach allows glycosylation data to be considered alongside preclinical performance data rather than treating glycosylation as an isolated analytical measurement.

The technology is particularly relevant to complex glycoproteins, including viral antigens, antibodies, and other biologics in which glycosylation can influence protein structure, stability, function, immune recognition, and therapeutic performance, Kemp said.