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Mao et al. (1) published a paper describing a 3D structure of uncleaved, trimeric HIV-1 envelope glycoprotein (Env) at ∼6-Å resolution, following a similar paper last year on the same structure at ∼11-Å resolution (2). Examination of these two papers leads me to doubt that the structures presented are results of a reliable cryo-electron microscopic analysis of purified HIV-1 Env trimers. An underlying assumption in structure determination by cryo-electron microscopy is that there is demonstrable evidence that the micrographs contain images of the relevant proteins, although their mere existence in no way guarantees that a structure at 6 Å, or even at 11 Å, can be obtained. The raw electron micrographs presented by Mao et al. (1, 2) do not provide convincing evidence for the presence of molecular images of HIV-1 Env trimers [compare fig. 1A from Mao et al. (1) with fig. 1B from Harris et al. (3), where trimers are clearly visible in the images]. I am therefore concerned that the authors have fallen into the well-known reference-bias trap in image processing by recovering what looks like a real structure starting from images of random noise. HIV-1 envelope glycoprotein structures determined by cryo-electron microscopy. (A) Electron micrograph presented in Mao et al. (1) with putative gp160 trimers circled. (B) For …

Structure of trimeric HIV-1 envelope glycoproteins