Gavilimomab

This study aimed to determine bone level changes after 5–6 years of follow‐up for a large group of one‐stage dental implants consecutively placed in private practice. Potential confounding factors influencing crestal bone loss (CBL) were also assessed.

A total of 378 transmucosal Straumann® implants in 174 patients were examined radiographically. Half of the study population (189 implants) had a titanium plasma sprayed (TPS) surface, and the other half (189 implants) were sandblasted and acid‐etched (SLA). Mean CBL was measured from 5 to 6 years post‐operative radiographs on the basis of known implant landmarks. Correlations of increased CBL with various independent variables were also investigated. Statistical analyses were performed using generalized estimating equations.

Radiographic measurements showed a CBL ≤ 1.5 mm for 65% of studied implants. A CBL > 1.5 mm was found for 28% of implants, while 7% of implants had a CBL ≥ 3 mm. Three factors significantly influenced CBL (P < 0.05): implant surface texture (TPS > SLA), smoking status (smokers > non‐smokers), and implant location (anterior > posterior).

CBL was ≤1.5 mm after 5–6 years for the majority of followed implants. For implants with a CBL > 1.5 mm, statistically significant correlations were found for TPS surface type, anterior jaw locations, and smoking. Implant length did not influence CBL.

The structure of VRC01 in complex with the HIV-1 gp120 core reveals that this broadly neutralizing CD4 binding site (CD4bs) antibody partially mimics the interaction of the primary virus receptor, CD4, with gp120. Here, we extended the investigation of the VRC01-gp120 core interaction to the biologically relevant viral spike to better understand the mechanism of VRC01-mediated neutralization and to define viral elements associated with neutralization resistance. In contrast to the interaction of CD4 or the CD4bs monoclonal antibody (MAb) b12 with the HIV-1 envelope glycoprotein (Env), occlusion of the VRC01 epitope by quaternary constraints was not a major factor limiting neutralization. Mutagenesis studies indicated that VRC01 contacts within the gp120 loop D, the CD4 binding loop, and the V5 region were necessary for optimal VRC01 neutralization, as suggested by the crystal structure. In contrast to interactions with the soluble gp120 monomer, VRC01 interaction with the native viral spike did not occur in a CD4-like manner; VRC01 did not induce gp120 shedding from the Env spike or enhance gp41 membrane proximal external region (MPER)-directed antibody binding to the Env spike. Finally, VRC01 did not display significant reactivity with human antigens, boding well for potential in vivo applications. The data indicate that VRC01 interacts with gp120 in the context of the functional spike in a manner distinct from that of CD4. It achieves potent neutralization by precisely targeting the CD4bs without requiring alterations of Env spike configuration and by avoiding steric constraints imposed by the quaternary structure of the functional Env spike.