Tau protein aggregation is a hallmark of over 20 diseases including Alzheimer’s Disease and frontotemporal lobar degeneration (FTLD) and is correlated with the progressive predictable patterns of degeneration observed in these neurodegenerative disorders. It has been hypothesised that extracellular vesicles (EVs) traffic tau to recipient cells which can induce tau aggregation and facilitate disease spread. Tau trafficking via EVs derived from cells in culture and mouse models has been investigated, however it remains to be seen whether EVs derived from human brain tissue can facilitate tau spread. Previously, the study of EVs has been hampered due to difficulties in enriching for EVs from solid tissues, this difficulty has only recently been overcome. By performing a recently developed brain derived EV enrichment technique, transmission electron microscopy and immunoblotting techniques, we enriched for and characterised, EVs derived from human FTLD frontal cortex tissue. Using Fluorescence Resonance Energy Transfer (FRET) flow cytometry we quantified tau aggregate formation in tau biosensor cells treated with human brain derived EVs. We have determined that the majority of extracellular seed-competent tau is not released in association with endosome-derived EVs in FTLD, but with a separate EV subpopulation. Our study offers insight into the mechanism of tau spread in FTLD and other tauopathies by demonstrating that exosomes have a minor role in tau transmission relative to high-density EVs that are enriched in seed-component tau.