Modelling parasite impacts of aquaculture on wild fish: The case of the salmon louse (Lepeophtheirus salmonis) on out-migrating wild Atlantic salmon (Salmo salar) smolt.

For effective wild salmon (Salmo salar) conservation in areas where aquaculture of salmon is practiced it is necessary to identify where the key parasite, the salmon louse (Lepeophtheirus salmonis), will have an impact on these wild salmon. A simple modelling structure is implemented in a sample system in Scotland for assessing interaction between wild salmon and salmon lice from salmon farms. The model is demonstrated for case studies of smolt sizes and migration routes through salmon lice concentration fields derived for average farm loads from 2018 to 2020. Lice modelling describes production and distribution of lice, infection rates on hosts and biological development of lice. The modelling framework allows explicit assessment of the relationships between lice production, lice concentration and impact on hosts as they grow and migrate. Lice distribution in the environment is determined using a kernel model, which summarises mixing in a complex hydrodynamic system. Smolt modelling describes their initial size, growth and migration pathways. This is illustrated for a set of parameter values applied to 10 cm, 12.5 cm and 15 cm salmon smolts. We found that salmon lice impact depends on initial size of host, smaller smolts will be more susceptible, while larger smolts are less impacted by a given number of lice encounters and migrate more rapidly. This modelling framework can be adapted to allow evaluation of threshold concentrations of lice in the water that should not be exceeded to avoid impacts on smolt populations.

ADAP is an upstream regulator that precedes SLP-76 at sites of TCR engagement and stabilizes signaling microclusters.

Antigen recognition by the T cell receptor (TCR) directs the assembly of essential signaling complexes known as SLP-76 (also known as LCP2) microclusters. Here, we show that the interaction of the adhesion and degranulation-promoting adaptor protein (ADAP; also known as FYB1) with SLP-76 enables the formation of persistent microclusters and the stabilization of T cell contacts, promotes integrin-independent adhesion and enables the upregulation of CD69. By analyzing point mutants and using a novel phospho-specific antibody, we show that Y595 is essential for normal ADAP function, that virtually all tyrosine phosphorylation of ADAP is restricted to a Y595-phosphorylated (pY595) pool, and that multivalent interactions between the SLP-76 SH2 domain and its binding sites in ADAP are required to sustain ADAP phosphorylation. Although pY595 ADAP enters SLP-76 microclusters, non-phosphorylated ADAP is enriched in protrusive actin-rich structures. The pre-positioning of ADAP at the contact sites generated by these structures favors the retention of nascent SLP-76 oligomers and their assembly into persistent microclusters. Although ADAP is frequently depicted as an effector of SLP-76, our findings reveal that ADAP acts upstream of SLP-76 to convert labile, Ca2+-competent microclusters into stable adhesive junctions with enhanced signaling potential.