Abstract: The molecular chaperones of small heat shock proteins (sHSPs) are key components that contribute to nematode survival in higher temperatures stress response. In heat shock, the sHSPs help the cell survival by the way of cell repair. A Bursaphelenchus xylophilus sHSP16A gene, Bx-sHSP16A, were found and well studied. The sHSP16A conserved motif “F-polar-R-polar-aromatic-x-L-P” and “I/L-x-I” were found in Bx-sHSP16A. Bx-sHSP16A has the chaperonelike functions. Bx-sHSP16A interact with many proteins, well studies of those proteins will help us understand the pathway related with sHSPs. In the Bx-sHSP16A dimer, the C terminus` “I/L-x-I” of the subunit A binding with the groove of the subunit B. These results indicated that Bx-sHSP16As could form oligomer. The chaperone activity of the Bx-sHSP16As oligomer has been postulated to coincide with the exposure of hydrophobic interface sites after a temperature-regulated subunit exchange or dissociation of the oligomer.