Question: What are the biological roles proposed for proteins containing the SPRY domain?

Context:
monkey TRIM5α SPRY domain recognizes multiple epitopes that span several capsid monomers on the surface of the HIV-1 mature viral core
These properties, which may enhance resistance of TRIM5α to capsid mutations, result in relatively low affinity of the individual SPRY domains for the capsid
RIM5α is a retroviral restriction factor, in which the B30.2 (SPRY) and coiled-coil domains cooperate to determine the specificity of TRIM5α-mediated capture of retroviral capsids
function of the SPRY/B30.2 domain proteins involved in innate immunity
SPRY domain is a protein interaction module found in 77 murine and ~100 human proteins, and is implicated in important biological pathways, including those that regulate innate and adaptive immunity
TRIM5α) is a potent antiviral protein that restricts infection by HIV-1 and other retroviruses
 TRIM5α recognizes the lattice of the retrovirus capsid through its B30.2 (PRY/SPRY) domain in a species-specific manner
binding of the PRY-SPRY domain from the TRIM50 C-terminal region to phosphatidylinositol species, suggesting that TRIM50 is involved in vesicular dynamics by sensing the phosphorylated state of phosphoinositol lipids
TRIM50 seems to play an essential role in tubulovesicular dynamics
TRIM67 regulates Ras signaling via degradation of 80K-H, leading to neural differentiation including neuritogenesis
TRIM67, which has a TRIM motif, an FN3 domain and a SPRY domain, is highly expressed in the cerebellum
Vasa coding region is sufficient for its selective enrichment and find that gustavus, the B30.2/SPRY and SOCS box domain gene
We propose that Gustavus has a conserved, positive regulatory role in Vasa protein accumulation during embryonic development
two zebrafish genes, SSB-1 and SSB-4 (SPRY domain SOCS box proteins
We hypothesize that SSB-4 plays a role in the early development of germ cells
SPRY domain of Pyrin, mutated in familial Mediterranean fever patients, interacts with inflammasome components and inhibits proIL-1beta processing
TRIM proteins may be conducive to the convergent evolution of virus-restricting factors.
SPRY and B30.2 protein domains. Evolution of a component of immune defence
. The combination of SPRY and PRY to produce B30.2 domains may have been selected and maintained as a component of immune defence
 evolution of primate TRIM5alpha, a gene restricting HIV-1 infection
The SPRY domain of TRIM5alpha, which may be responsible for recognition of incoming viral capsids showed higher nonsynonymous/synonymous substitution ratios than the non-SPRY domain, indicating that the adaptive evolution of TRIM5alpha in primates might be an innate strategy developed in defending retrovirus infection during primate evolutio
The results are consistent with a role for TRIM5alpha in innate immunity against retroviruses
B30.2(SPRY) domain of the retroviral restriction factor TRIM5alpha
primate TRIM5alpha identifies a critical species-specific retroviral restriction domain
By using functional studies of chimeric TRIM5alpha genes, we show that this patch is generally essential for retroviral restriction and is responsible for most of the species-specific antiretroviral restriction activity
SPRY protein domain
Heterozygotes for gus or a deletion including gus produce embryos with fewer pole cells and posterior patterning defects
SPRY-domain and SOCS-box containing protein, GUSTAVUS.

Answer: defence against retroviral infection
innate and adaptative immunity
vesicular trafficking
neural differentiation
embryonic development
Exact answer: defence against retroviral infection, immunity, vesicular trafficking, neural differentiation, embryonic development