Phages are viruses that infect bacteria. They affect various microbe-mediated processes that drive biogeochemical cycling on a global scale. Their influence depends on whether the infection is lysogenic or lytic. Temperate phages have the potential to execute both infection types and thus frequently switch their infection modes in nature, potentially causing substantial impacts on the host-phage community and relevant biogeochemical cycling. Understanding the regulating factors and outcomes of temperate phage life cycle transition is thus fundamental for evaluating their ecological impacts. This review thus systematically summarizes the effects of various factors affecting temperate phage life cycle decisions in both culturable phage-host systems and natural environments. The review further elucidates the ecological implications of the life cycle transition of temperate phages with an emphasis on phage/host fitness, host-phage dynamics, microbe diversity and evolution, and biogeochemical cycles.

Since the discovery of fluorescent proteins (FPs), their rich fluorescence spectra and photochemical properties have promoted widespread biological research applications. FPs can be classified into green fluorescent protein (GFP) and its derivates, red fluorescent protein (RFP) and its derivates, and near-infrared FPs. With the continuous development of FPs, antibodies targeting FPs have emerged. The antibody, a class of immunoglobulin, is the main component of humoral immunity that explicitly recognizes and binds antigens. Monoclonal antibody, originating from a single B cell, has been widely applied in immunoassay, in vitro diagnostics, and drug development. The nanobody is a new type of antibody entirely composed of the variable domain of a heavy-chain antibody. Compared with conventional antibodies, these small and stable nanobodies can be expressed and functional in living cells. In addition, they can easily access grooves, seams, or hidden antigenic epitopes on the surface of the target. This review provides an overview of various FPs, the research progress of their antibodies, particularly nanobodies, and advanced applications of nanobodies targeting FPs. This review will be helpful for further research on nanobodies targeting FPs, making FPs more valuable in biological research.

The fat covered by fat globule membrane is scattered in a water phase rich in lactose and milky protein, forming the original emulsion structure of milk. In order to develop low-fat milk products with good performance or dairy products with nutritional reinforcement, the original emulsion structure of milk can be restructured. According to the type of lipid and emulsion structure in milk, the remolded emulsion structure can be divided into three types: restructured single emulsion structure, mixed emulsion structure, and double emulsion structure. The restructured single emulsion structure refers to the introduction of another kind of lipid to skim milk, and the mixed emulsion structure refers to adding another type of oil or oil-in-water (O/W) emulsion to milk containing certain levels of milk fat, whose final emulsion structure is still O/W emulsion. In contrast, the double emulsion structure of milk is a more complicated structural remodeling method, which is usually performed by introducing W/O emulsion into skim milk (W₂) to obtain milk containing (water-in-oil-in-water) W₁/O/W₂ emulsion structure in order to encapsulate more diverse nutrients. Causal statistical analysis was used in this review, based on previous studies on remodeling the emulsion structures in milk and its gelling products. In addition, some common processing technologies (including heat treatment, high-pressure treatment, homogenization, ultrasonic treatment, micro-fluidization, freezing and membrane emulsification) may also have a certain impact on the microstructure and properties of milk and its gelling products with four different emulsion structures. These processing technologies can change the size of the dispersed phase of milk, the composition and structure of the interfacial layer, and the composition and morphology of the aqueous phase substance, so as to regulate the shelf-life, stability, and sensory properties of the final milk products. This research on the restructuring of the emulsion structure of milk is not only a cutting-edge topic in the field of food science, but also a powerful driving force in promoting the transformation and upgrading of the dairy industry to achieve high-quality and multi-functional dairy products, in order to meet the diversified needs of consumers for health and taste.

The receptor-binding domain (RBD) of the SARS-CoV-2 spike protein is the major target for antibody therapeutics. Shark-derived variable domains of new antigen receptors (VNARs) are the smallest antibody fragments with flexible paratopes that can recognize protein motifs inaccessible to classical antibodies. This study reported four VNARs binders (JM-2, JM-5, JM-17, and JM-18) isolated from Chiloscyllium plagiosum immunized with SARS-CoV-2 RBD. Biolayer interferometry showed that the VNARs bound to the RBD with an affinity K_D ranging from 38.5 to 2720 nM, and their Fc fusions had over ten times improved affinity. Gel filtration chromatography revealed that JM-2-Fc, JM-5-Fc, and JM-18-Fc could form stable complexes with RBD in solution. In addition, five bi-paratopic VNARs, named JM-2-5, JM-2-17, JM-2-18, JM-5-18, and JM-17-18, were constructed by fusing two VNARs targeting distinct RBD epitopes based on epitope grouping results. All these bi-paratopic VNARs except for JM-5-18 showed higher RBD binding affinities than its component VNARs, and their Fc fusions exhibited further enhanced binding affinities, with JM-2-5-Fc, JM-2-17-Fc, JM-2-18-Fc, and JM-5-18-Fc having K_D values lower than 1 pM. Among these Fc fusions of bi-paratopic VNARs, JM-2-5-Fc, JM-2-17-Fc, and JM-2-18-Fc could block the angiotensin-converting enzyme 2 (ACE2) binding to the RBD of SARS-CoV-2 wildtype, Delta, Omicron, and SARS-CoV, with inhibition rates of 48.9~84.3%. Therefore, these high-affinity VNAR binders showed promise as detectors and therapeutics of COVID-19.