Lab+Life Scientist Apr/May 2022

Page 30

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HEK cells vs CHO cells in recombinant antibody production What’s the better choice?

The demand for therapeutic proteins is constantly growing and gives further reason for continuing the development of high-quality protein production technologies. Mammalian cell lines are the preferred choice to create recombinant proteins, in particular Chinese hamster ovary (CHO) cells and human embryonic kidney (HEK or HEK293) cells.

H

also known to be a reliable base for the translation

CHO cells: the workhorse of the biopharma industry

and processing of proteins and can therefore be

CHO cells are the workhorse of the biopharma

used for many experiments. As Dr Desmond

industry — over 70% of biopharmaceuticals, and

Schofield, Director of Business Development at

almost all antibodies, are produced within this cell

evitria, explained:

line. A review by Dumont et al found that only five

suitable for various transfection methods. They are

owever, with the higher demand

also comes a higher confusion of which cell line to pick for one’s own studies. HEK cells are known to

“HEK cells are a well-established and

be very popular due to their easy handling and use

commonly used host for transient expression in

for protein production, while CHO cells are the

R&D labs. They are easy to transiently transfect

CHO cells are robust hosts that grow well

most used mammalian production cell line within

using a variety of different and low-cost methods,

in suspension culture, can easily be adapted

the biopharmaceutical industry. Due to the many

and produce fully human glycosylation patterns.

to serum-free media, and can produce and

possibilities as well as advantages and disadvantages,

Their transfectability is the main reason for their

secrete recombinant antibodies in the multi-

it can be quite troubling to decide which cells would

widespread use and popularity.”

gram scale. As they are hamster-derived cells,

FDA-approved biotherapeutics are produced within HEK, and 50 with CHO (as of 2016).

However, HEK cells are rarely used beyond

they are less susceptible to contamination

research settings, due to several limitations. One of

by human viruses, but still perform human-

the biggest obstacles a researcher could face when

compatible glycosylation. They do lack α[2-6]

HEK: common host for transient expression in R&D labs

using HEK cells is that they are difficult to grow in

sialyltransferase α[1-3/4] fucosyltransferases, and

large-scale, serum-free cultures. They form clumps

they produce glycans that are not expressed in

HEK cells are popular protein expression hosts

that hinder nutrient transfer and growth, and cause

humans, namely α-gal and NGNA. However, the

among researchers due to their fast transfectability

heterogeneity in the culture process. Furthermore,

glycosylation modifications from these changes

and protein production. Adding to that, HEK cells

these clumps reduce the efficiency of downstream

are rarely required for the function of a given

are easy to reproduce and to maintain and are

processing and purification.

product, and the additional glycans only occur

serve specific research the best. This article is designed to help scientists make the right choice.

30 | LAB+LIFE SCIENTIST - Apr/May 2022

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