Autophagy degrades unnecessary organelles and misfolded protein aggregates(1), as well as cytoplasm-invading bacteria(2). Nevertheless, the bacteria Listeria monocytogenes efficiently escapes autophagy(3,4). We show here that recruitment of the Arp2/3 complex and Ena/VASP, via the bacterial ActA protein, to the bacterial surface disguises the bacteria from autophagic recognition, an activity that is independent of the ability to mediate bacterial motility. L. monocytogenes expressing ActA mutants that lack the ability to recruit the host proteins initially underwent ubiquitylation, followed by recruitment of p62 (also known as SQSTM1) and LC3, before finally undergoing autophagy. The ability of ActA to mediate protection from ubiquitylation was further demonstrated by generating aggregate-prone GFP-ActA-Q79C and GFP ActA-170* chimaeras, consisting of GFP (green fluorescent protein), the ActA protein and segments of polyQ(5) or Golgi membrane protein GCP170 (ref. 6). GFP-ActA-Q79C and GFP-ActA-170* formed aggregates in the host cell cytoplasm, however, these ActA-containing aggregates were not targeted for association with ubiquitin and p62. Our findings indicate that ActA-mediated host protein recruitment is a unique bacterial disguise tactic to escape from autophagy.