Three-dimensional structure of a Nanobody® (modeled on the VHH with pdb-code 1U0Q, Cambillau et al). The target molecule is recognized by the surface formed by three hypervariable regions located at the top of the molecule (in green, cyan and blue). Hallmarks, amino acid residues that further differentiate a camelid VHH from a human VH, can be located at different positions within the framework regions, and here are coloured red, pink and magenta.

Home R & D Nanobody® Bibliography > Alternative Routes of Administration

Nanobody® Bibliography

Alternative Routes of Administration

Muyldermans S.  Single domain camel antibodies: current status.  J Biotechnol. 2001 Jun; 74 (4): 277-302.

Gibbs WW.  Nanobodies.  Sci Am. 2005 Aug; 293 (2): 78-83.

Harmsen MM, van Solt CB, van Zijderveld-van Bemmel AM, Niewold TA, van Zijderveld FG.  Selection and optimization of proteolytically stable llama single-domain antibody fragments for oral immunotherapy.  Appl Microbiol Biotechnol. 2006 Feb 1; 1-8.

Kruger C, Hultberg A, Marcotte H, Hermans P, Bezemer S, Frenken LG, Hammarstrom L.  Therapeutic effect of llama derived VHH fragments against Streptococcus mutans on the development of dental caries.  Appl Microbiol Biotechnol. 2006 Apr 25.

van der Vaart JM, Pant N, Wolvers D, Bezemer S, Hermans PW, Bellamy K, Sarker SA, van der Logt CP, Svensson L, Verrips CT, Hammarstrom L, van Klinken BJ.  Reduction in morbidity of rotavirus induced diarrhoea in mice by yeast produced monovalent llama-derived antibody fragments.  Vaccine. 2006 May 8; 24 (19): 4130-7.

Pant N, Hultberg A, Zhao Y, Svensson L, Pan-Hammarstrom Q, Johansen K, Pouwels PH, Ruggeri FM, Hermans P, Frenken L, Boren T, Marcotte H, Hammarstrom L. Lactobacili expressing variable domain of llama heavy-chain antibody fragments (lactobodies) confer protection against rotavirus-induced diarrhea. J Infect Dis. 2006 Dec 1; 194 (11): 1580-8