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Table 2 Description of sdAbs and variants

From: Selection, characterization, and thermal stabilization of llama single domain antibodies towards Ebola virus glycoprotein

Clone name

Description of mutations

Charge Δ

EBOV-GP-G6

Original clone

0

EBOV-GP-G6-neg+

Disulfide addition: A54C, I78C

− 1

FR1 changes: Q5V, A6E

EBOV-GP-H7

Original clone

0

EBOV-GP-H7-neg+

Disulfide addition: A54C, I78C

− 1

FR1 changes: Q5V, A6E

EBOV-GP-A8

Original clone

0

EBOV-GP-A8-neg+

Disulfide addition: A54C, I78C

− 2

FR1 changes: Q5V, A6E, A13V, G17D

EBOV-GP-A8-fneg+

Disulfide addition: A54C, I78C

− 2

FR1 changes: Q5V, A6E, A13V, G17D

Unpaired Cys mutated: C106S

  1. Three of the GP binding sdAbs showing the highest melting temperatures and/or best affinities were subject to mutagenesis to improve their stability. Mutations included addition of a non-canonical disulfide bond, changes to FR1 that added negative charge, and “fixing” clone EBOV-GP-A8 by mutating an unpaired Cys