Serum albumin first appeared in early vertebrates and is present in the plasma of all mammals. Its canonical structure supported by a conserved set of disulfide bridges is maintained in all mammalian serum albumins and any changes in sequence are highly correlated with evolution of the species. Previous structural investigations of mammalian serum albumins have only concentrated on human serum albumin (HSA), most likely as a consequence of crystallization and diffraction difficulties. Here, the crystal structures of serum albumins isolated from bovine, equine and leporine blood plasma are reported. The structure of bovine serum albumin (BSA) was determined at 2.47 A resolution, two crystal structures of equine serum albumin (ESA) were determined at resolutions of 2.32 and 2.04 A, and that of leporine serum albumin (LSA) was determined at 2.27 A resolution. These structures were compared in detail with the structure of HSA. The ligand-binding pockets in BSA, ESA and LSA revealed different amino-acid compositions and conformations in comparison to HSA in some cases; however, much more significant differences were observed on the surface of the molecules. BSA, which is one of the most extensively utilized proteins in laboratory practice and is used as an HSA substitute in many experiments, exhibits only 75.8% identity compared with HSA. The higher resolution crystal structure of ESA highlights the binding properties of this protein because it includes several bound compounds from the crystallization solution that provide additional structural information about potential ligand-binding pockets.

Structures of bovine, equine and leporine serum albumin.

The availability of allergen molecules ('components') from several protein families has advanced our understanding of immunoglobulin E (IgE)-mediated responses and enabled 'component-resolved diagnosis' (CRD). The European Academy of Allergy and Clinical Immunology (EAACI) Molecular Allergology User's Guide (MAUG) provides comprehensive information on important allergens and describes the diagnostic options using CRD. Part A of the EAACI MAUG introduces allergen molecules, families, composition of extracts, databases, and diagnostic IgE, skin, and basophil tests. Singleplex and multiplex IgE assays with components improve both sensitivity for low-abundance allergens and analytical specificity; IgE to individual allergens can yield information on clinical risks and distinguish cross-reactivity from true primary sensitization. Part B discusses the clinical and molecular aspects of IgE-mediated allergies to foods (including nuts, seeds, legumes, fruits, vegetables, cereal grains, milk, egg, meat, fish, and shellfish), inhalants (pollen, mold spores, mites, and animal dander), and Hymenoptera venom. Diagnostic algorithms and short case histories provide useful information for the clinical workup of allergic individuals targeted for CRD. Part C covers protein families containing ubiquitous, highly cross-reactive panallergens from plant (lipid transfer proteins, polcalcins, PR-10, profilins) and animal sources (lipocalins, parvalbumins, serum albumins, tropomyosins) and explains their diagnostic and clinical utility. Part D lists 100 important allergen molecules. In conclusion, IgE-mediated reactions and allergic diseases, including allergic rhinoconjunctivitis, asthma, food reactions, and insect sting reactions, are discussed from a novel molecular perspective. The EAACI MAUG documents the rapid progression of molecular allergology from basic research to its integration into clinical practice, a quantum leap in the management of allergic patients.

EAACI Molecular Allergology User's Guide.

Anti-PEG antibodies in the clinic: Current issues and beyond PEGylation.

Binding of transition metal ions to albumin: sites, affinities and rates.

Current trends in interfacial polymerization chemistry

Structural and immunologic characterization of bovine, horse, and rabbit serum albumins.

This meta-analysis investigated the association between age-related hearing loss and structural neuroanatomy, specifically changes to gray matter volume. Hearing loss is associated with increased risk of cognitive decline. Hence, understanding the effects of hearing loss in older age on brain health is essential. We reviewed studies which compared older participants with hearing loss (age-related hearing loss: ARHL) to older adults without clinical hearing loss (no-ARHL), on neuroanatomical outcomes, specifically gray matter (GM) volume as measured by magnetic resonance imaging. A total of five studies met the inclusion criteria, three of which were included in an analysis of whole-brain gray matter volume (ARHL group n = 113; no-ARHL group n = 138), and three were included in analyses of lobe-wise gray matter volume (ARHL group n = 139; no-ARHL group n = 162). Effect-size seed-based d mapping software was employed for whole-brain and lobe-wise analysis of gray matter volume. The analysis indicated there was no significant difference between adults with ARHL compared to those with no-ARHL in whole-brain gray matter volume. Due to lacking stereotactic coordinates, the level of gray matter in specific neuroanatomical locations could only be observed at lobe-level. These data indicate that adults with ARHL show increased gray matter atrophy in the temporal lobe only (not in occipital, parietal, or frontal), compared to adults with no-ARHL. The implications for theoretical frameworks of the hearing loss and cognitive decline relationship are discussed in relation to the results. This meta-analysis was pre-registered on PROSPERO (CRD42021265375). Systematic Review Registration: https://www.crd.york.ac.uk/prospero/display_record.php?RecordID=265375, PROSPERO CRD42021265375.

Kamila Jablonska

Papers

Structural and immunologic characterization of bovine, horse, and rabbit serum albumins.

The impact of age-related hearing loss on structural neuroanatomy: A meta-analysis