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Earthquake-triggered landslides show three important characteristics: they are often responsible for a considerable proportion of the damage sustained during mountain region earthquakes, they are non-randomly distributed across space, and they continue to evolve in the years after the earthquake. Despite this, planning for future earthquakes rarely takes into consideration either landslides or their evolution with time. Here we couple a unique timeseries of mapped landslides between 2014-2020 across the area of Nepal impacted by the 2015 Mw 7.8 Gorkha earthquake and a numerical landslide runout model overlain with building locations to examine how the distributions of both evolving landslide hazard and exposure intersect to generate a dynamic threat to buildings. The threat from landslide runout is shown to change in predictable ways after the earthquake, becoming more pronounced at mid- and lower-hillslope positions and remaining in the landscape for multiple years. Using the positions of our mapped landslides as a starting point, we can identify a priori the locations of 78% of buildings that were subsequently impacted by landslide debris. We show that landslide exposure and hazard vary from negligible to high, in relative terms, over lateral distances of as little as 10s of m. Our findings hold important implications for guiding reconstruction and for taking steps to reduce the risks from future earthquakes., Competing Interests: The authors have declared that no competing interests exist., (Copyright: © 2024 Arrell et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.)

We have identified the protein product of the Autographa californica nuclear polyhedrosis virus (AcMNPV) p143 gene by constructing a recombinant baculovirus overexpressing the gene product P143. The overexpressed protein exhibited a relative mobility of approximately 140 kDa and was stable for at least 12 hr after synthesis. Immunoblotting using a monoclonal antibody developed against the overexpressed protein identified a similar polypeptide in AcMNPV-infected cells which was detectable by 4 hr postinfection. P143 was present within infected cell nuclei at relatively constant amounts until at least 72 hr after infection, suggesting that P143 may perform other functions at late times after infection. P143, purified from infected cell nuclei by chromatography over hydroxylapatite and DNA cellulose, bound in a sequence-independent fashion to double-stranded but not to single-stranded DNA to form a ladder of retarded protein-DNA complexes. Together, these data are consistent with the essential role of P143 for viral DNA replication and suggest that P143 may function by direct binding to DNA.