Disputation: Hedda Johannesen

Doctoral candidate Hedda Johannesen at the Department of Biosciences will be defending the thesis "Unmasking the Assassin— A structural and functional analysis of the anti-tumour antibody 14F7: providing new insight into the NeuGc GM3 binding mechanism" for the degree of Philosophiae Doctor.

Profilepicture of Hedda Johannesen

Photo: Hedda Johannesen, UiO.

The disputation will be live streamed using Zoom. The host of the session will moderate the technicalities while the chair of the defence will moderate the disputation.

Ex auditorio questions: the chair of the defence will invite the audience to ask ex auditorio questions either written or oral. This can be requested by clicking "Participants" followed by clicking "Raise hand". 

The meeting opens for participation just before 2.00 PM, and closes for new participants approximately 15 minutes after the defense has begun.

Trial lecture

Time and place: August 12, 2020 2:00 PM,  Zoom

"Tumor targeted superantigens"

The meeting opens for participation just before 2.00 PM, and closes for new participants approximately 15 minutes after the trial lecture has begun.

Main research findings

14F7 – a universal cure for cancer?

Imagine how it would be if you could be cured from cancer without experiencing side effects such as nausea or losing your hair. For decades, scientists have worked towards finding a cancer-specific target that can be recognised by a drug: a drug that explicitly destroys the tumour without inducing harmful side effects.

One such cure could potentially be the antibody 14F7, which shows great promise as it binds to a variety of tumours with high specificity, without reacting with healthy tissues. 14F7 targets a sugar-coated lipid named NeuGc GM3, that most of us consume every day, but only cancer cells use it as protective coat.

In this work, we have discovered how this antibody recognises its cancer-associated target, NeuGc GM3, by X-rays. Additionally, we explored the drug-target interaction by model membrane systems. Combined, these results further validate the antibody 14F7’s potential as a diagnostic and therapeutic drug.

Illustration: Hedda Johannesen, UiO
Figure 1: Cartoon of 14F7 mAb and its binding to tumour cells. Heavy chains are coloured purple, light chains are deep blue and carbohydrates are depicted as white sticks. The mAb structure is generated as composite of 14F7 Fab (PDB: 1RIH), a human IgG1 Fc (PDP: 1IGY), and 14F7 scFv structure (PDB: 6S2I) containing the trisaccharide part of 14F7´s binding partner, the N-glycolyl GM3 ganglioside.

Illustration: Hedda Johannesen, UiO
Published July 31, 2020 9:31 AM - Last modified Aug. 12, 2020 8:07 AM