Objective: The purpose of this manuscript is to identify proteins exclusive to the inner ear based on published research to identify potential candidate biomarkers and guide future inner ear research. Data Sources: Literature on inner ear proteins published on Pubmed, Google Scholar, and Scopus was reviewed using key words such as “inner ear molecule,” “inner ear exclusive protein,” and several specific protein searches such as “prestin” based on findings from the initial searches. Study Selections: Studies were selected for abstract review based on title relevance, and full text was chosen for review based on abstract relevance. Several related studies cited in initially reviewed literature were also chosen to compile more detailed information on specific molecules with the goal of at least two to three published articles for each protein. Data Extraction & Synthesis: Proteins that were cited to have only been found within the inner ear were included in this review, including some proteins that were later identified outside the inner ear. Information regarding their size, location, function, and clinical significance was recorded. Conclusions: Based on this literature search, eight proteins exclusive to the inner ear were identified including otolin-1, otoconin 90/95, prestin, otoancorin, otogelin, α-tectorin, β-tectorin, and cochlin. Proteins initially found to be exclusive to the inner ear though later identified outside of the inner ear included oncomodulin, otospiralin, and otoraplin. This literature review may serve as a focused guide for future research on proteins exclusive to the inner ear as potential biomarkers for diseases of the inner ear.

The utilization of bioactive peptides in the development of highly selective and potent pharmacologic agents for the disruption of protein-protein interactions is appealing for drug discovery. It is known that HIV-1 entry into host cell is through a fusion process that is mediated by the trimeric viral glycoprotein gp120/41 which are derived from gp160 through proteolytic processing. Peptides derived from the HIV gp41 C-terminus have proven to be potent in inhibiting the fusion process. These peptides bind tightly to the hydrophobic pocket on gp-41 N-terminus which was previously identified as a potential inhibitor binding site. In this study, we introduced modified 23-residue C-peptides, 3 and 4, bearing a sulfono-γ-AA residue substitution and hydrocarbon stapling, respectively, which were developed for HIV-1 gp-41 N-terminus binding. Intriguingly, both 3 and 4 were capable of inhibiting envelope-mediated membrane fusion in cell-cell fusion assays at nanomolar potency. Our study reveals that sulfono-γ-AA modified peptides could be used for the development of more potent anti-HIV agents.

A 39-year-old male with chronic hydrocephalus requiring biventricular shunts presented with progressive pneumocephalus over several years. He showed no improvement following ventriculoperitoneal (VP) shunt revision and anterior skull base repair for a sphenoid dehiscence. Imaging continued to show worsening pneumocephalus with air tracking along the right facial nerve from the geniculate ganglion to the internal auditory canal (IAC). The patient then underwent tympanomastoidectomy and skull base reconstruction. Based on a search of published literature, this appears to be the first reported case of temporal bone pneumocephalus coursing through the IAC, unlike most cases associated with tegmen defects and middle fossa pneumocephalus.

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