Neurimmune announced today that preclinical data relating to its human antibody NI006 (NI301A) targeting transthyretin amyloid (ATTR) have been published in the current issue of Nature Communications. The paper “A human antibody selective for transthyretin amyloid removes cardiac amyloid through phagocytic immune cells” describes a monoclonal antibody that binds with high affinity selectively to disease-associated aggregated forms of ATTR.
NI006 was discovered by Neurimmune’s Reverse Translational MedicineTM (RTMTM) technology through a comprehensive analysis of memory B cell repertoires derived from healthy elderly subjects. The human antibody efficiently removed ATTR deposits from patient-derived myocardium tissues ex vivo, as well as patient-derived ATTR fibril grafts in mice in a dose- and time-dependent fashion.
“We are excited about these results which provide the scientific basis for the development of NI006 as a potential treatment for patients with ATTR cardiomyopathy”, said Jan Grimm, CSO of Neurimmune. “Reducing myocardial ATTR load is a therapeutic objective anticipated to translate into restored cardiac function.”
ATTR cardiomyopathy is a debilitating disease leading to heart failure and death. Extracellular myocardial ATTR deposits can accumulate in massive amounts impacting the mechanical properties of the myocardium such as diastolic relaxation followed by systolic impairments as the disease progresses. NI006 removes ATTR amyloid with the help of the immune system by recruiting phagocytic immune cells to ATTR deposits thereby targeting them for degradation.