1SJX

Three-Dimensional Structure of a Llama VHH Domain OE7 binding the cell wall protein Malf1

Summary for 1SJX

• Entry DOI: 10.2210/pdb1sjx/pdb
• Descriptor: immunoglobulin VH domain, (4S)-2-METHYL-2,4-PENTANEDIOL (3 entities in total)
• Functional Keywords: camelids antibody, heavy chain, dandruff, phage display, immune system
• Biological source: Lama glama (llama)
• Total number of polymer chains: 1
• Total formula weight: 13451.02

Authors

Dolk, E.,van der Vaart, M.,Hulsik, D.L.,Vriend, G.,de Haard, H.,Spinelli, S.,Cambillau, C.,Frenken, L.,Verrips, T. (deposition date: 2004-03-04, release date: 2005-03-15, Last modification date: 2024-11-13)

Primary citation

Dolk, E.,van der Vaart, M.,Hulsik, D.L.,Vriend, G.,de Haard, H.,Spinelli, S.,Cambillau, C.,Frenken, L.,Verrips, T.
Isolation of llama antibody fragments for prevention of dandruff by phage display in shampoo.
Appl.Environ.Microbiol., 71:442-450, 2005

PubMed Abstract: As part of research exploring the feasibility of using antibody fragments to inhibit the growth of organisms implicated in dandruff, we isolated antibody fragments that bind to a cell surface protein of Malassezia furfur in the presence of shampoo. We found that phage display of llama single-domain antibody fragments (VHHs) can be extended to very harsh conditions, such as the presence of shampoo containing nonionic and anionic surfactants. We selected several VHHs that bind to the cell wall protein Malf1 of M. furfur, a fungus implicated in causing dandruff. In addition to high stability in the presence of shampoo, these VHHs are also stable under other denaturing conditions, such as high urea concentrations. Many of the stable VHHs were found to contain arginine at position 44. Replacement of the native amino acid at position 44 with arginine in the most stable VHH that lacked this arginine resulted in a dramatic further increase in the stability. The combination of the unique properties of VHHs together with applied phage display and protein engineering is a powerful method for obtaining highly stable VHHs that can be used in a wide range of applications.

PubMed: 15640220
DOI: 10.1128/AEM.71.1.442-450.2005

Experimental method

X-RAY DIFFRACTION (2.2 Å)