Figure 6.

ASFV assembly and release (9). Changes in the virus particle morphology occur in virus factory (VF). (1) A104R is located in the core shell and involved in ASFV genome packaging. (2) p14 expression inhibition produces defective interference particles without a central nucleoid. (3) The core shell adsorbs on the inner membrane depending on pp220 N-bean acrylamide. (4) pp220 hydrolysis separates the core shell from the inner capsule membrane, thus concentrating, condensing, and merging the nucleus. (5) pp220 and pp62 hydrolysis inhibition leads to non-nuclear or non-infectious virus particle production. (6) ASFV proteolytic enzyme pS273R catalyzes protease processing of polyprotein precursors. (7) Proteins that affect pp220 and pp62 hydrolysis include pB602L and p17. (8) The assembly of the major capsid protein p72 requires the assistance of B602L-encoded molecular chaperone. (9) p54 expression inhibition interrupts endoplasmic reticulum (ER) transfer to virus assembly site. (10) P54 proteins interact with microtube power complexes by connecting directly to dynein. Newly-synthesized viruses are linked to kinesins, which drives the virus to move from VF to extracellular. (11) p17 plays an important role in capsule precursor conversion into an icosahedron intermediate. (12) pB602L synthesis inhibition forms abnormal “zip-like” structure instead of icosahedron. (13) Membrane protein pB438L expression inhibition forms abnormal tubular structure instead of icosahedron.