Ebola Virus Ectodomain

This is a 3D print of x-ray crystallography datasets PDB IDs: 3CSY, 2EBO  The protein surface color coding is defined by the protein’s Hydrophobicity. To delineate the different chains, we have colored the GP2-Glycoprotein-plasma membrane a green colors. The model can be printed in a variety of materials and sizes.

Protein Description

“Ebolavirus (EBOV) is a highly virulent pathogen capable of causing a severe hemorrhagic fever with 50–90% lethality. The EBOV glycoprotein (GP) is the only virally expressed protein on the virion surface and is critical for attachment to host cells and catalysis of membrane fusion. Hence, the EBOV GP is a critical component of vaccines as well as a target of neutralizing antibodies and inhibitors of attachment and fusion. The crystal structure of the Zaire ebolavirus GP in its trimeric, prefusion conformation (3 GP1 plus 3 GP2) in complex with a neutralizing antibody fragment, derived from a human survivor of the 1995 Kikwit outbreak, was recently determined.


This is the first near-complete structure of any filovirus glycoprotein. The overall molecular architecture of the Zaire ebolavirus GP and its role in viral entry and membrane fusion are discussed in this article.”  — NCBI Citation

3D Animation


Ebola Virus Ectodomain in complex with Human Antibodies from Biologic Discovery on Vimeo.

The ebola virus has a natural enemy, the human immune system. Those lucky enough to survey this deadly virus produce an antibody which identifies the virus for destruction. The above animation shows these antibodies attached to the ectodomains of the virus.

Structural Mechanisms of Nucleosome Recognition by Linker Histones

“The EBOV envelope GP directly mediates binding of the virion to the host cell. A number of cellular factors, including DC-SIGN/L-SIGN [68,69], LSECtin [70,71], hMGL [72], β-integrins [73] and Tyro3 family receptors [74], have been implicated as attachment factors, however, none of these proteins individually are necessary and sufficient for viral entry. Hence, a critical cell-surface receptor responsible for EBOV attachment has yet to be identified, despite significant effort. It appears that EBOV enters through a receptor-mediated endocytotic mechanism, but it is still unclear whether clathrin-, caveolae- or cholesterol-dependent processes are used. Recombinant systems using pseudotyped retro-virus particles with ZEBOV GP and live virus studies using chemical inhibitors of clathrin- and caveolae-mediated endocytosis point to the use of caveolae and clathrin in EBOV entry [75,76]. However, cells lacking in caveolae can still be infected with EBOV [77].” – NCBI Citation


Image Gallery

Model Description

This is the full scale version of the Ebola Virus Ectodomain model, printed at 9.962 cm x 14.658 cm x 9.564 cm. Please see below for a link to the small scale version.

Material Sample Preview

We can print our Biologic Models in a variety of materials and sizes. Check out digital previews of the model if printed in different materials.

Purchase Model

Small Size

Purchase a SMALL scale version of the Ebola Virus Ectodomain model through Shapeways and select from multiple material options.

Medium Size

Purchase a FULL scale version of the Ebola Virus Ectodomain model through Shapeways and select from multiple material options.