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To identify the effect of nitrogen (N) nutrition on the dynamic photosynthesis of rice plants, a pot experiment was conducted under two N conditions. The leaf N and chlorophyll levels, as well as steady–state photosynthesis, were significantly increased under high N. After the transition from saturating to low light levels, decreases in the induction state (IS%) of leaf photosynthesis (A) and stomatal conductance (gs) were more severe under low than under high N supply. After the transition from low to flecked irradiance, the times to 90% of maximum A (T90%A) were significantly longer under low than under high N supply. Under flecked irradiance, the maximum A under saturating light (Amax–fleck) and the steady–state A under low light (Amin–fleck) were both lower than those under uniform irradiance (Asat and Ainitial). Under high N supply, Amax–fleck was 14.12% lower than Asat, while it was 22.80% lower under low N supply. The higher IS%, shorter T90%A, and the lower depression of Amax–fleck from Asat under high N supply led to a less carbon loss compared with under a low N supply. Therefore, we concluded that N can improve the rapid response of photosynthesis to changing irradiance.

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BackgroundNon-structural protein 1 (NS1) is a multifunctional protein and a crucial regulatory factor in the replication and pathogenesis of avian influenza virus (AIV). Studies have shown that NS1 can interact with a variety of host proteins to modulate the viral life cycle. We previously generated a monoclonal antibody against NS1 protein; In the current research study, using this antibody, we immunoprecipitated host proteins that interact with NS1 to better understand the roles played by NS1 in communications between virus and host.ResultsCo-immunoprecipitation experiments identified annexin A2 (ANXA2) as a target molecule interacting with NS1. Results from confocal laser scanning microscopy indicated that NS1 co-localized with ANXA2 in the cell cytoplasm. Overexpression of ANXA2 significantly increased the titer of H5N1 subtype HPAIV, whereas siRNA-mediated knockdown of ANXA2 markedly inhibited the expression of viral proteins and reduced the progeny virus titer.ConclusionsOur results indicate that ANXA2 interacts with NS1 and ANXA2 expression increases HPAIV replication.Electronic supplementary materialThe online version of this article (10.1186/s12866-017-1097-0) contains supplementary material, which is available to authorized users.

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