Single domain antibodies: promising experimental and therapeutic tools in infection and immunity.
Antibodies are important tools for experimental research and medical applications. Most antibodies are composed of two heavy and two light chains. Both chains contribute to the antigen-binding site which is usually flat or concave. In addition to these conventional antibodies, llamas, other camelids, and sharks also produce antibodies composed only of heavy chains. The antigen-binding site of these unusual heavy chain antibodies (hcAbs) is formed only by a single domain, designated VHH in camelid hcAbs and VNAR in shark hcAbs. VHH and VNAR are easily produced as recombinant proteins, designated single domain antibodies (sdAbs) or nanobodies. The CDR3 region of these sdAbs possesses the extraordinary capacity to form long fingerlike extensions that can extend into cavities on antigens, e.g., the active site crevice of enzymes. Other advantageous features of nanobodies include their small size, high solubility, thermal stability, refolding capacity, and good tissue penetration in vivo. Here we review the results of several recent proof-of-principle studies that open the exciting perspective of using sdAbs for modulating immune functions and for targeting toxins and microbes.
Wesolowski
Janusz
J
Institute of Immunology, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.
Alzogaray
Vanina
V
Reyelt
Jan
J
Unger
Mandy
M
Juarez
Karla
K
Urrutia
Mariela
M
Cauerhff
Ana
A
Danquah
Welbeck
W
Rissiek
Björn
B
Scheuplein
Felix
F
Schwarz
Nicole
N
Adriouch
Sahil
S
Boyer
Olivier
O
Seman
Michel
M
Licea
Alexei
A
Serreze
David V
DV
Goldbaum
Fernando A
FA
Haag
Friedrich
F
Koch-Nolte
Friedrich
F
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000737:chemistry* / Q000276:immunology; D002161:Camelids, New World / Q000276:immunology; D022801:Complementarity Determining Regions / Q000737:chemistry / Q000276:immunology; D007143:Immunoglobulin Heavy Chains / Q000737:chemistry* / Q000276:immunology; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry / Q000276:immunology; D016415:Sequence Alignment; D012754:Sharks / Q000276:immunology
D000906:Antibodies; D022801:Complementarity Determining Regions; D007143:Immunoglobulin Heavy Chains; D011994:Recombinant Proteins